Skip Navigation
Skip to contents

Journal of Microbiology : Journal of Microbiology

OPEN ACCESS
SEARCH
Search
Advanced Search
mobile menu button

Search

Page Path
HOME > Search
52 "protease"
Filter
Filter
Article category
Keywords
More +
Publication year
More +
Authors
Funded articles
Research Article
LasB activation in Pseudomonas aeruginosa: Quorum sensing-mediated release of an auto-activation inhibitor
Cheol Seung Lee, Xi-Hui Li, Chae-Ran Jeon, Joon-Hee Lee
J. Microbiol. 2025;63(2):e2411005.   Published online February 27, 2025
DOI: https://doi.org/10.71150/jm.2411005
  • 1,673 View
  • 76 Download
  • 1 Scopus
AbstractAbstract PDF

Pseudomonas aeruginosa secretes three major proteases: elastase B (LasB), protease IV (PIV), and elastase A (LasA), which play crucial roles in infection and pathogenesis. These proteases are activated sequentially from LasB in a proteolytic cascade, and LasB was previously thought to undergo auto-activation. However, our previous study suggested that LasB cannot auto-activate independently but requires additional quorum sensing (QS)-dependent factors for activation, as LasB remained inactive in QS-deficient P. aeruginosa (QS-) even under artificial overexpression. In this study, we provide evidence for the existence of a LasB inhibitor in QS- mutants: inactive LasB overexpressed in QS- strains was in its processed form and could be reactivated upon purification; when full-length LasB was overexpressed in Escherichia coli, a heterologous bacterium lacking both LasB activators and inhibitors, the protein underwent normal processing and activation; and purified active LasB was significantly inhibited by culture supernatant (CS) from QS- strains but not by CS from QS+ strains. These findings demonstrate that a LasB inhibitor exists in QS- strains, and in its absence, LasB can undergo auto-activation without requiring an activator. Based on these results, we propose an updated hypothesis: the QS-dependent LasB activator functions by removing the LasB inhibitor rather than acting directly on LasB itself, thus preventing premature LasB activation until QS response is initiated.
Journal Articles
Ten Novel Species Belonging to the Genus Flavobacterium, Isolated from Freshwater Environments: F. praedii sp. nov., F. marginilacus sp. nov., F. aestivum sp. nov., F. flavigenum sp. nov., F. luteolum sp. nov., F. gelatinilyticum sp. nov., F. aquiphilum sp. nov., F. limnophilum sp. nov., F. lacustre
Hyunyoung Jo , Miri S. Park , Yeonjung Lim , Ilnam Kang , Jang-Cheon Cho
J. Microbiol. 2023;61(5):495-510.   Published online May 23, 2023
DOI: https://doi.org/10.1007/s12275-023-00054-4
  • 554 View
  • 1 Download
  • 10 Web of Science
  • 10 Crossref
AbstractAbstract PDF
Eleven bacterial strains were isolated from freshwater environments and identified as Flavobacterium based on 16S rRNA gene sequence analyses. Complete genome sequences of the 11 strains ranged from 3.45 to 5.83 Mb with G + C contents of 33.41–37.31%. The average nucleotide identity (ANI) values showed that strains IMCC34515T and IMCC34518 belonged to the same species, while the other nine strains represented each separate species. The ANI values between the strains and their closest Flavobacterium species exhibited ≤ 91.76%, indicating they represent each novel species. All strains had similar characteristics such as being Gram-stain-negative, rod-shaped, and contained iso-C15:0 as the predominant fatty acid, menaquinone-6 as the respiratory quinone, and phosphatidylethanolamine and aminolipids as major polar lipids. Genomic, phylogenetic, and phenotypic characterization confirmed that the 11 strains were distinct from previously recognized Flavobacterium species. Therefore, Flavobacterium praedii sp. nov. (IMCC34515T = KACC 22282T = NBRC 114937T), Flavobacterium marginilacus sp. nov. (IMCC34673T = KACC 22284T = NBRC 114940T), Flavobacterium aestivum sp. nov. (IMCC34774T = KACC 22285T = NBRC 114941T), Flavobacterium flavigenum sp. nov. (IMCC34775T = KACC22286T = NBRC 114942T), Flavobacterium luteolum sp. nov. (IMCC34776T = KACC 22287T = NBRC 114943T), Flavobacterium gelatinilyticum sp. nov. (IMCC34777T = KACC 22288T = NBRC 114944T), Flavobacterium aquiphilum sp.nov. (IMCC34779T = KACC 22289T = NBRC 114945T), Flavobacterium limnophilum sp. nov. (IMCC36791T = KACC22290T = NBRC 114947T), Flavobacterium lacustre sp. nov. (IMCC36792T = KACC 22291T = NBRC 114948T), and Flavobacterium eburneipallidum sp. nov. (IMCC36793T = KACC 22292T = NBRC 114949T) are proposed as novel species.

Citations

Citations to this article as recorded by  
  • Indoor pollution of funeral homes and potential health risk of workers: A case study in central China
    Jinjun Ye, Zhengtao Ai, Lup Wai Chew
    Building and Environment.2025; 272: 112677.     CrossRef
  • Flavobacterium magnesitis sp. nov. and Flavobacterium zubiriense sp. nov., two novel Flavobacterium species isolated from alkaline magnesite residues
    Leonor Matos, Lorrie Maccarrio, Ana Paula Chung, Diogo N. Proença, Søren Sørensen, Paula V. Morais, Romeu Francisco
    International Journal of Systematic and Evolutionary Microbiology .2025;[Epub]     CrossRef
  • Comparative genomics and evolutionary insights into zeaxanthin biosynthesis in two novel Flavobacterium species
    Ye Zhuo, Chun-Zhi Jin, Chang-Soo Lee, Kee-Sun Shin, Hyung-Gwan Lee
    BMC Microbiology.2025;[Epub]     CrossRef
  • Flavobacterium adiutor sp. nov., a newly identified freshwater bacterium potentially supporting Microcystis growth via oxidative stress reduction
    Ve Van Le, So-Ra Ko, Yuna Shin, Kyunghyun Kim, Sang-Ah Lee, Chi-Yong Ahn
    International Journal of Systematic and Evolutionary Microbiology .2025;[Epub]     CrossRef
  • Comprehensive genome analysis of five novel flavobacteria: Flavobacterium piscisymbiosum sp. nov., Flavobacterium pisciphilum sp. nov., Flavobacterium flavipigmentatum sp. nov., Flavobacterium lipolyticum sp. nov. and Flavobacterium cupriresistens sp. nov
    Izzet Burcin Saticioglu, Hilal Ay, Soner Altun, Nihed Ajmi, Enes Said Gunduz, Huban Gocmen, Muhammed Duman
    Systematic and Applied Microbiology.2024; 47(4): 126518.     CrossRef
  • Leuconostoc aquikimchii sp. nov., a Lactic Acid Bacterium Isolated from Cabbage Watery Kimchi
    Subin Kim, Se Hee Lee, Ki Hyun Kim, Misun Yun
    Journal of Microbiology.2024; 62(12): 1089.     CrossRef
  • Overproduction of Xanthophyll Pigment in Flavobacterium sp. JSWR-1 under Optimized Culture Conditions
    Jegadeesh Raman, Young-Joon Ko, Jeong-Seon Kim, Da-Hye Kim, Soo-Jin Kim
    Journal of Microbiology and Biotechnology.2024; 34(3): 710.     CrossRef
  • Flavobacterium rivulicola sp. nov., Isolated from a Freshwater Stream
    Sumin Kim, Miri S. Park, Ilnam Kang, Jang-Cheon Cho
    Current Microbiology.2024;[Epub]     CrossRef
  • Congregibacter variabilis sp. nov. and Congregibacter brevis sp. nov. Within the OM60/NOR5 Clade, Isolated from Seawater, and Emended Description of the Genus Congregibacter
    Hyeonsu Tak, Miri S. Park, Hyerim Cho, Yeonjung Lim, Jang-Cheon Cho
    Journal of Microbiology.2024; 62(9): 739.     CrossRef
  • Validation List no. 213. Valid publication of new names and new combinations effectively published outside the IJSEM
    Aharon Oren, Markus Göker
    International Journal of Systematic and Evolutionary Microbiology .2023;[Epub]     CrossRef
Alpha‑Hemolysin from Staphylococcus aureus Obstructs Yeast‑Hyphae Switching and Diminishes Pathogenicity in Candida albicans
Xiaoyu Yu , Yinhe Mao , Guangbo Li , Xianwei Wu , Qiankun Xuan , Simin Yang , Xiaoqing Chen , Qi Cao , Jian Guo , Jinhu Guo , Wenjuan Wu
J. Microbiol. 2023;61(2):233-243.   Published online February 9, 2023
DOI: https://doi.org/10.1007/s12275-022-00006-4
  • 455 View
  • 0 Download
  • 4 Web of Science
  • 2 Crossref
AbstractAbstract PDF
The use of antibiotics can disrupt the body’s natural balance and increase the susteptibility of patients towards fungal infections. Candida albicans is a dimorphic opportunistic fungal pathogen with niches similar to those of bacteria. Our aim was to study the interaction between this pathogen and bacteria to facilitate the control of C. albicans infection. Alpha-hemolysin (Hla), a protein secreted from Staphylococcus aureus, causes cell wall damage and impedes the yeast–hyphae transition in C. albicans. Mechanistically, Hla stimulation triggered the formation of reactive oxygen species that damaged the cell wall and mitochondria of C. albicans. The cell cycle was arrested in the G0/G1 phase, CDC42 was downregulated, and Ywp1 was upregulated, disrupting yeast hyphae switching. Subsequently, hyphae development was inhibited. In mouse models, C. albicans pretreated with Hla reduced the C. albicans burden in skin and vaginal mucosal infections, suggesting that S. aureus Hla can inhibit hyphal development and reduce the pathogenicity of candidiasis in vivo.

Citations

Citations to this article as recorded by  
  • The therapeutic potential of phage-based antifungal treatment: strategies, mechanisms, and prospects
    Haowen Xiao, Jiayue Xie, Zhiping Luo, Xiaomin Yu, Jumei Zeng, Yuqing Li
    Critical Reviews in Microbiology.2025; : 1.     CrossRef
  • Candida albicans and Candida glabrata : global priority pathogens
    Myrto Katsipoulaki, Mark H. T. Stappers, Dhara Malavia-Jones, Sascha Brunke, Bernhard Hube, Neil A. R. Gow, Joseph Heitman
    Microbiology and Molecular Biology Reviews.2024;[Epub]     CrossRef
Expression and purification of intracrine human FGF 11 and study of its FGFR-dependent biological activity
Kyeong Won Lee , Young Jun An , Janet Lee , Ye-Eun Jung , In Young Ko , Jonghwa Jin , Ji Hoon Park , Won Kyu Lee , Kiweon Cha , Sun-Shin Cha , Jung-Hyun Lee , Hyung-Soon Yim
J. Microbiol. 2022;60(11):1086-1094.   Published online November 1, 2022
DOI: https://doi.org/10.1007/s12275-022-2406-3
  • 387 View
  • 0 Download
  • 7 Web of Science
  • 6 Crossref
AbstractAbstract PDF
Fibroblast growth factor 11 (FGF11) is one of intracrine FGFs (iFGFs), which function within cells. Unlike canonical FGFs, FGF11 remains intracellularly and plays biological roles in FGF receptor (FGFR)-independent manner. Here, we established an expression system of recombinant FGF11 proteins in E. coli and investigated whether the extracellular administration of FGF11 can activate cellular signaling. Human FGF11 has two isoforms, FGF11a and FGF11b, depending on the presence of nuclear localization sequences (NLSs) in the N-terminus. Because these two isoforms are unstable, we prepared an FGF11a-Mut by substituting three cysteine residues in the NLS with serine and FGF11b-ΔC with C-terminal truncation. The introduction of mutation in the NLS improved the solubility of FGF11 prepared from E. coli. Exogenous addition of FGF11b and FGF11b-ΔC to BALB3T3 increased cell proliferation, while FGF11a-Mut exerted no effect. FGF11b-ΔC showed higher cell proliferation activity and FGFR signaling than FGF11b. The cell-proliferating activities of FGF11b and FGF11b-ΔC were blocked by an FGFR1 inhibitor or a recombinant FGFR1, confirming the FGFR1- dependent extracellular activity of FGF11b. The analysis of circular dichroism suggested that the C-terminus of FGF11 has an α-helical structure, which may affect its interaction with FGFR1. These results suggest that the N-and C-terminus of recombinant FGF11 are involved in the activation of FGFR1. The above results provide novel insights into the function and mechanism of FGF11 that may aid the development of useful ligands for FGFR regulation.

Citations

Citations to this article as recorded by  
  • Fibroblast Growth Factors: Roles and Emerging Therapeutic Applications
    Gaëtane Ternier, Kaynat Shahzad, Oshadi Edirisinghe, Patience Okoto, Zeina Alraawi, Shivakumar Sonnaila, Phuc Phan, Paul D. Adams, Suresh K. Thallapuranam
    Current Drug Targets.2025; 26(8): 551.     CrossRef
  • Production and purification of recombinant long protein isoforms of FGF11 subfamily
    Martyna Biadun, Szymon Sidor, Marta Kalka, Radoslaw Karelus, Martyna Sochacka, Daniel Krowarsch, Lukasz Opalinski, Malgorzata Zakrzewska
    Journal of Biotechnology.2025; 403: 9.     CrossRef
  • Function of orthologous fibroblast growth factor 11 protein in angiogenesis and immunomodulatory after spinal cord injury
    Congcong Zou, Min Chen, Qian Zhao, Letong Wang, Luyang Ye, Xiaolei Meng, Xiaokun Li, Yanming Zuo, Zhouguang Wang
    International Journal of Biological Macromolecules.2025; 330: 148106.     CrossRef
  • Glycosylation of FGF/FGFR: An underrated sweet code regulating cellular signaling programs
    Aleksandra Gędaj, Paulina Gregorczyk, Dominika Żukowska, Aleksandra Chorążewska, Krzysztof Ciura, Marta Kalka, Natalia Porębska, Łukasz Opaliński
    Cytokine & Growth Factor Reviews.2024; 77: 39.     CrossRef
  • FGF homologous factors are secreted from cells to induce FGFR‐mediated anti‐apoptotic response
    Martyna Biadun, Martyna Sochacka, Radoslaw Karelus, Karolina Baran, Aleksandra Czyrek, Jacek Otlewski, Daniel Krowarsch, Lukasz Opalinski, Malgorzata Zakrzewska
    The FASEB Journal.2023;[Epub]     CrossRef
  • FGF/FGFR1 system in paired breast tumor-adjacent and tumor tissues, associations with mammographic breast density and tumor characteristics
    Öykü Boraka, Marie Klintman, Johan Vallon-Christersson, Sophia Zackrisson, Per Hall, Signe Borgquist, Ann H. Rosendahl
    Frontiers in Oncology.2023;[Epub]     CrossRef
Mutational analysis on stable expression and LasB inhibition of LasB propeptide in Pseudomonas aeruginosa
Youngsun Shin , Xi-Hui Li , Cheol Seung Lee , Joon-Hee Lee
J. Microbiol. 2022;60(7):727-734.   Published online May 25, 2022
DOI: https://doi.org/10.1007/s12275-022-1671-5
  • 366 View
  • 0 Download
  • 1 Web of Science
  • 1 Crossref
AbstractAbstract PDF
Three major proteases, elastase B (LasB), protease IV (PIV), and elastase A (LasA) expressed in Pseudomonas aeruginosa play important roles in infections and pathogeneses. These are activated by a proteolytic cascade initiated by the activation of LasB. In this study, we investigated whether LasB could be inhibited using its propeptide (LasBpp). Although LasA and PIV were inhibited by their propeptides, LasB was not inhibited by purified LasBpp because LasB degraded LasBpp. To address this problem, mutant LasBpp variants were constructed to obtain a mutant LasBpp resistant to LasB degradation. A C-terminal deletion series of LasBpp was tested in vivo, and two positive candidates, T2 and T2-1, were selected. However, both caused growth retardation and were unstably expressed in vivo. Since deleting the C-terminal end of LasBpp significantly affected its stable expression, substitution mutations were introduced at the two amino acids near the truncation site of T2-1. The resulting mutants, LasBppE172D, LasBppG173A, and LasBppE172DG173A, significantly diminished LasB activity when overexpressed in vivo and were stably expressed in MW1, a quorum sensing mutant that does not produce LasB. In vitro analysis showed that purified LasBppE172DG173A inhibited LasB activity to a small extent. Summarizing, Cterminal modification of LasBpp profoundly affected the stable expression of LasBpp, and little enhanced the ability of LasBpp to resist degradation by LasB.

Citations

Citations to this article as recorded by  
  • LasB activation in Pseudomonas aeruginosa: Quorum sensing-mediated release of an auto-activation inhibitor
    Cheol Seung Lee, Xi-Hui Li, Chae-Ran Jeon, Joon-Hee Lee
    Journal of Microbiology.2025; 63(2): e2411005.     CrossRef
Short-chain fatty acids inhibit the biofilm formation of Streptococcus gordonii through negative regulation of competence-stimulating peptide signaling pathway
Taehwan Park , Jintaek Im , A Reum Kim , Dongwook Lee , Sungho Jeong , Cheol-Heui Yun , Seung Hyun Han
J. Microbiol. 2021;59(12):1142-1149.   Published online December 4, 2021
DOI: https://doi.org/10.1007/s12275-021-1576-8
  • 500 View
  • 2 Download
  • 18 Web of Science
  • 19 Crossref
AbstractAbstract PDF
Streptococcus gordonii, a Gram-positive commensal bacterium, is an opportunistic pathogen closely related to initiation and progression of various oral diseases, such as periodontitis and dental caries. Its biofilm formation is linked with the development of such diseases by enhanced resistance against antimicrobial treatment or host immunity. In the present study, we investigated the effect of short-chain fatty acids (SCFAs) on the biofilm formation of S. gordonii. SCFAs, including sodium acetate (NaA), sodium propionate (NaP), and sodium butyrate (NaB), showed an effective inhibitory activity on the biofilm formation of S. gordonii without reduction in bacterial growth. SCFAs suppressed S. gordonii biofilm formation at early time points whereas SCFAs did not affect its preformed biofilm. A quorum-sensing system mediated by competence-stimulating peptide (CSP) is known to regulate biofilm formation of streptococci. Interestingly, SCFAs substantially decreased mRNA expression of comD and comE, which are CSP-sensor and its response regulator responsible for CSP pathway, respectively. Although S. gordonii biofilm formation was enhanced by exogenous synthetic CSP treatment, such effect was not observed in the presence of SCFAs. Collectively, these results suggest that SCFAs have an anti-biofilm activity on S. gordonii through inhibiting comD and comE expression which results in negative regulation of CSP quorum-sensing system. SCFAs could be an effective anti-biofilm agent against S. gordonii for the prevention of oral diseases.

Citations

Citations to this article as recorded by  
  • Recent progress in understanding the role of bacterial extracellular DNA: focus on dental biofilm
    Fengxue Geng, Junchao Liu, Jinwen Liu, Ze Lu, Yaping Pan
    Critical Reviews in Microbiology.2025; 51(5): 898.     CrossRef
  • Potential effects of prebiotic fibers on dental caries: a systematic review
    Constanza E. Fernández, Catalina Maturana‐Valenzuela, Nicol Rojas‐Castillo, Bob Rosier
    Journal of the Science of Food and Agriculture.2025; 105(11): 5640.     CrossRef
  • Formation, architecture, and persistence of oral biofilms: recent scientific discoveries and new strategies for their regulation
    Chengyuan Lv, Ziyi Wang, Zehui Li, Xialing Shi, Mingming Xiao, Yan Xu
    Frontiers in Microbiology.2025;[Epub]     CrossRef
  • The human skin microbiome: from metagenomes to therapeutics
    Julia Oh, Anita Y. Voigt
    Nature Reviews Microbiology.2025;[Epub]     CrossRef
  • Serotype-Dependent Inhibition of Streptococcus pneumoniae Growth by Short-Chain Fatty Acids
    Suwon Lim, Dongwook Lee, Sungho Jeong, Jeong Woo Park, Jintaek Im, Bokeum Choi, Donghyun Gwak, Cheol-Heui Yun, Ho Seong Seo, Seung Hyun Han
    Journal of Microbiology and Biotechnology.2024; 34(1): 47.     CrossRef
  • Comprehensive Multi-Omic Evaluation of the Microbiota and Metabolites in the Colons of Diverse Swine Breeds
    Yanbin Zhu, Guangming Sun, Yangji Cidan, Bin Shi, Zhankun Tan, Jian Zhang, Wangdui Basang
    Animals.2024; 14(8): 1221.     CrossRef
  • Effects of Epigallocatechin gallate on Biofilm adherence and Glycolytic pH in Streptococcus gordonii
    Prawati Nuraini, Dimas Prasetianto Wicaksono, Ardianti Maartrina Dewi, Adinda Ayu Fitriana, Sili Han
    Research Journal of Pharmacy and Technology.2024; : 4711.     CrossRef
  • Oral Pathogens and Their Antibiotics from Marine Organisms: A Systematic Review of New Drugs for Novel Drug Targets
    Sehyeok Im, Jun Hyuck Lee, Youn-Soo Shim
    Journal of Dental Hygiene Science.2024; 24(2): 84.     CrossRef
  • Effects of the gut microbiota and its metabolite short-chain fatty acids on endometriosis
    Menghe Liu, Ru Peng, Chunfang Tian, Jianping Shi, Jiannan Ma, Ruiwen Shi, Xiao Qi, Rongwei Zhao, Haibin Guan
    Frontiers in Cellular and Infection Microbiology.2024;[Epub]     CrossRef
  • Butyrate potentiates Enterococcus faecalis lipoteichoic acid-induced inflammasome activation via histone deacetylase inhibition
    Ok-Jin Park, Ye-Eun Ha, Ju-Ri Sim, Dongwook Lee, Eun-Hye Lee, Sun-Young Kim, Cheol-Heui Yun, Seung Hyun Han
    Cell Death Discovery.2023;[Epub]     CrossRef
  • Gut microbiota short-chain fatty acids and their impact on the host thyroid function and diseases
    María José Mendoza-León, Ashutosh K. Mangalam, Alejandro Regaldiz, Enrique González-Madrid, Ma. Andreina Rangel-Ramírez, Oscar Álvarez-Mardonez, Omar P. Vallejos, Constanza Méndez, Susan M. Bueno, Felipe Melo-González, Yorley Duarte, Ma. Cecilia Opazo, Al
    Frontiers in Endocrinology.2023;[Epub]     CrossRef
  • Crosstalk between microbial biofilms in the gastrointestinal tract and chronic mucosa diseases
    Yumeng Wang, Shixi Xu, Qiurong He, Kun Sun, Xiaowan Wang, Xiaorui Zhang, Yuqing Li, Jumei Zeng
    Frontiers in Microbiology.2023;[Epub]     CrossRef
  • Listening to enteric bacteria from the perspective of antibiotic alternatives in animal husbandry
    Leli Wang, Yiru Zhang, Juan Xu, Qingqing Shi, Yao Peng, Cimin Long, Lan Li, Yulong Yin
    The Innovation Life.2023; 1(2): 100022.     CrossRef
  • The Complicated Relationship of Short-Chain Fatty Acids and Oral Microbiome: A Narrative Review
    Georgy E. Leonov, Yurgita R. Varaeva, Elena N. Livantsova, Antonina V. Starodubova
    Biomedicines.2023; 11(10): 2749.     CrossRef
  • Social networking at the microbiome-host interface
    Richard J. Lamont, George Hajishengallis, Hyun Koo, Anthony R. Richardson
    Infection and Immunity.2023;[Epub]     CrossRef
  • Making Sense of Quorum Sensing at the Intestinal Mucosal Interface
    Friederike Uhlig, Niall P. Hyland
    Cells.2022; 11(11): 1734.     CrossRef
  • Food-Grade Bacteria Combat Pathogens by Blocking AHL-Mediated Quorum Sensing and Biofilm Formation
    Kirsi Savijoki, Paola San-Martin-Galindo, Katriina Pitkänen, Minnamari Edelmann, Annika Sillanpää, Cim van der Velde, Ilkka Miettinen, Jayendra Z. Patel, Jari Yli-Kauhaluoma, Mataleena Parikka, Adyary Fallarero, Pekka Varmanen
    Foods.2022; 12(1): 90.     CrossRef
  • Innate immunity and microbial dysbiosis in hidradenitis suppurativa – vicious cycle of chronic inflammation
    Divya Chopra, Rachel A. Arens, Watcharee Amornpairoj, Michelle A. Lowes, Marjana Tomic-Canic, Natasa Strbo, Hadar Lev-Tov, Irena Pastar
    Frontiers in Immunology.2022;[Epub]     CrossRef
  • Drugs for the Quorum Sensing Inhibition of Oral Biofilm: New Frontiers and Insights in the Treatment of Periodontitis
    Alessandro Polizzi, Martina Donzella, Giada Nicolosi, Simona Santonocito, Paolo Pesce, Gaetano Isola
    Pharmaceutics.2022; 14(12): 2740.     CrossRef
The role of Jacalin-related lectin gene AOL_s00083g511 in the development and pathogenicity of the nematophagous fungus Arthrobotrys oligospora
Xinyuan Dong , Jiali Si , Guanghui Zhang , Zhen Shen , Li Zhang , Kangliang Sheng , Jingmin Wang , Xiaowei Kong , Xiangdong Zha , Yongzhong Wang
J. Microbiol. 2021;59(8):736-745.   Published online July 5, 2021
DOI: https://doi.org/10.1007/s12275-021-1029-4
  • 416 View
  • 0 Download
  • 4 Web of Science
  • 3 Crossref
AbstractAbstract PDF
Arthrobotrys oligospora is a model species of nematophagous fungi and has great potential for the biological control of nematode diseases. Lectin is a protein that binds to carbohydrates and their complexes with high specificity, which mediates recognition events in various physiological and pathological processes. This study aimed to investigate the role of the Jacalin-related lectin (JRL) gene, AOL_s00083g511, in A. oligospora development. Through a homology recombination approach, we obtained the AOL_s00083g511 knockout mutant strain (Δg511). Next, the biological characteristics of the Δg511 mutant strain, including growth rate, conidia germination rate, adaptation to environmental stresses, and nematocidal activity, were compared with those of the wild-type (WT) strain. The results showed that the JRL gene AOL_ s00083g511 did not affect fungal growth, conidia germination, 3D-trap formation, and the ability of A. oligospora to prey on nematodes significantly. We speculate that this phenomenon may be caused by a loss of the key β1–β2 loops in the AOL_ s00083g511-encoded JRL domain and an intrinsic genetic compensation of AOL_s00083g511 in this fungus. The growth rates of both strains on high salt or surfactant media were similar; however, in the strong oxidation medium, the growth rate of the Δg511 mutant was significantly lower than that of the WT strain, indicating that AOL_s00083g511 might play a role in oxidative stress resistance. These findings provide a basis for further analysis of the related functions of the JRL gene in A. oligospora and their potential roles in the biological control of nematodes in the future.

Citations

Citations to this article as recorded by  
  • Function discovery of a non-ribosomal peptide synthetase-like encoding gene in the nematode-trapping fungus Arthrobotrys oligospora
    Tiantian Gu, Hengqian Lu, Huiwen Liu, Guanghui Zhang, Yongzhong Wang
    Frontiers in Microbiology.2023;[Epub]     CrossRef
  • The fucose-specific lectin gene AOL_s00054g276 affects trap formation and nematocidal activity of the nematophagous fungus Arthrobotrys oligospora
    Jiali Si, Xinyuan Dong, Guanghui Zhang, Hengqian Lu, Kaijing Tang, Li Zhang, Xiaowei Kong, Kangliang Sheng, Jingmin Wang, Xiangdong Zha, Yongzhong Wang
    FEMS Microbiology Letters.2022;[Epub]     CrossRef
  • Phospholipase C (AoPLC2) regulates mycelial development, trap morphogenesis, and pathogenicity of the nematode-trapping fungus Arthrobotrys oligospora
    Meihua Xie, Ni Ma, Na Bai, Meichen Zhu, Ke-Qin Zhang, Jinkui Yang
    Journal of Applied Microbiology.2022; 132(3): 2144.     CrossRef
Whole genome analysis of Aspergillus sojae SMF 134 supports its merits as a starter for soybean fermentation
Kang Uk Kim , Kyung Min Kim , Yong-Ho Choi , Byung-Serk Hurh , Inhyung Lee
J. Microbiol. 2019;57(10):874-883.   Published online June 27, 2019
DOI: https://doi.org/10.1007/s12275-019-9152-1
  • 442 View
  • 0 Download
  • 15 Web of Science
  • 15 Crossref
AbstractAbstract PDF
Aspergillus sojae is a koji (starter) mold that has been applied for food fermentation in Asia. The whole genome of A. sojae SMF 134, which was isolated from meju (Korean soybean fermented brick), was analyzed at the genomic level to evaluate its potential as a starter for soybean fermentation. The genome size was 40.1 Mbp, which was expected to be composed of eight chromosomes with 13,748 ORFs. Strain SMF 134 had a total of 151 protease genes, among which two more leucine aminopeptidase (lap) genes were found in addition to the previously known lap1, and three γ-glutamyltranspeptidase (ggt) genes were newly identified. Such genomic characteristics of SMF 134 with many protease and flavor-related (lap and ggt) genes support its merits as a starter for soybean fermentation. In addition, this first complete genome of A. sojae will allow for further genetic studies to better understand the production of various enzymes, including proteases, LAPs, and GGTs, as well as other characteristics as a starter mold for soybean fermentation.

Citations

Citations to this article as recorded by  
  • Population Genomics of Aspergillus sojae is Shaped by the Food Environment
    Kimberly L Acevedo, Elizabeth Eaton, Julia Leite, Shu Zhao, Katherine Chacon-Vargas, Colin M McCarthy, Dasol Choi, Samuel O’Donnell, Emile Gluck-Thaler, Jae-Hyuk Yu, John G Gibbons, Rebecca Zufall
    Genome Biology and Evolution.2025;[Epub]     CrossRef
  • Starter molds and multi-enzyme catalysis in koji fermentation of soy sauce brewing: A review
    Yihao Liu, Guangru Sun, Jingyao Li, Peng Cheng, Qian Song, Wen Lv, Chunling Wang
    Food Research International.2024; 184: 114273.     CrossRef
  • Phenotypic, Genomic, and Transcriptomic Comparison of Industrial Aspergillus oryzae Used in Chinese and Japanese Soy Sauce: Analysis of Key Proteolytic Enzymes Produced by Koji Molds
    Lijie Zhang, Le Kang, Yan Xu, Yanbin Yin
    Microbiology Spectrum.2023;[Epub]     CrossRef
  • Characteristics of the soy sauce taste and koji enzyme profiles as affected by soybean traits
    Yimin Chen, Mouming Zhao, Yunzi Feng
    Food Bioscience.2023; 53: 102776.     CrossRef
  • Comparative proteome and volatile metabolome analysis of Aspergillus oryzae 3.042 and Aspergillus sojae 3.495 during koji fermentation
    Jingyao Li, Bin Liu, Xiaojuan Feng, Mengli Zhang, Tingting Ding, Yue Zhao, Chunling Wang
    Food Research International.2023; 165: 112527.     CrossRef
  • CRISPR/Cas9 genome editing for comparative genetic analysis related to soy sauce brewing in Aspergillus sojae industrial strains
    Takayuki Igarashi, Takuya Katayama, Jun-ichi Maruyama
    Bioscience, Biotechnology, and Biochemistry.2023; 87(10): 1236.     CrossRef
  • Untargeted metabolomic profiling of Aspergillus sojae 3.495 and Aspergillus oryzae 3.042 fermented soy sauce koji and effect on moromi fermentation flavor
    Jingyao Li, Chengguo Sun, Zhanyu Shen, Yutong Tian, Fanghua Mo, Binghui Wang, Bin Liu, Chunling Wang
    LWT.2023; 184: 115027.     CrossRef
  • Identification of Virulence Factors in Entomopathogenic Aspergillus flavus Isolated from Naturally Infected Rhipicephalus microplus
    Cesar A. Arreguin-Perez, Estefan Miranda-Miranda, Jorge Luis Folch-Mallol, Raquel Cossío-Bayúgar
    Microorganisms.2023; 11(8): 2107.     CrossRef
  • Are Current Aspergillus sojae Strains Originated from a Native Aflatoxigenic Aspergillus Species Population Also Present in California?
    Perng-Kuang Chang, Sui Sheng T. Hua
    Mycobiology.2023; 51(3): 139.     CrossRef
  • Investigating the origin of subtelomeric and centromeric AT-rich elements in Aspergillus flavus
    Arthur J. Lustig, Cecile Fairhead
    PLOS ONE.2023; 18(2): e0279148.     CrossRef
  • Whole-genome sequence of an Aspergillus parasiticus strain isolated from Kenyan soil
    Alexandra Schamann, Rolf Geisen, Markus Schmidt-Heydt, Antonis Rokas
    Microbiology Resource Announcements.2023;[Epub]     CrossRef
  • Ethno-microbiology of Tempe, an Indonesian fungal-fermented soybean food and Koji, a Japanese fungal starter culture
    Jyoti P Tamang, Anu Anupma, Headstar Nakibapher Jones Shangpliang
    Current Opinion in Food Science.2022; 48: 100912.     CrossRef
  • Regulation of Conidiogenesis in Aspergillus flavus
    He-Jin Cho, Sung-Hun Son, Wanping Chen, Ye-Eun Son, Inhyung Lee, Jae-Hyuk Yu, Hee-Soo Park
    Cells.2022; 11(18): 2796.     CrossRef
  • High molecular weight DNA extraction methods lead to high quality filamentous ascomycete fungal genome assemblies using Oxford Nanopore sequencing
    Celine Petersen, Trine Sørensen, Klaus R. Westphal, Lavinia I. Fechete, Teis E. Sondergaard, Jens L. Sørensen, Kåre L. Nielsen
    Microbial Genomics .2022;[Epub]     CrossRef
  • Koji Molds for Japanese Soy Sauce Brewing: Characteristics and Key Enzymes
    Kotaro Ito, Asahi Matsuyama
    Journal of Fungi.2021; 7(8): 658.     CrossRef
A rule governing the FtsH-mediated proteolysis of the MgtC virulence protein from Salmonella enterica serovar Typhimurium
Jonghyun Baek , Eunna Choi , Eun-Jin Lee
J. Microbiol. 2018;56(8):565-570.   Published online July 25, 2018
DOI: https://doi.org/10.1007/s12275-018-8245-6
  • 383 View
  • 0 Download
  • 6 Crossref
AbstractAbstract PDF
A tightly controlled turnover of membrane proteins is required for lipid bilayer stability, cell metabolism, and cell viability. Among the energy-dependent AAA+ proteases in Salmonella, FtsH is the only membrane-bound protease that contributes to the quality control of membrane proteins. FtsH preferentially degrades the C-terminus or N-terminus of misfolded, misassembled, or damaged proteins to maintain physiological functions. We found that FtsH hydrolyzes the Salmonella MgtC virulence protein when we substitute the MgtC 226th Trp, which is well conserved in other intracellular pathogens and normally protects MgtC from the FtsH-mediated proteolysis. Here we investigate a rule determining the FtsHmediated proteolysis of the MgtC protein at Trp226 residue. Substitution of MgtC tryptophan 226th residue to alanine, glycine, or tyrosine leads to MgtC proteolysis in a manner dependent on the FtsH protease whereas substitution to phenylalanine, methionine, isoleucine, leucine, or valine resists MgtC degradation by FtsH. These data indicate that a large and hydrophobic side chain at 226th residue is required for protection from the FtsH-mediated MgtC proteolysis.

Citations

Citations to this article as recorded by  
  • Edwardsiella piscicida requires SecY homeostasis facilitated by FtsH and YccA for stress resistance and virulence
    Qingjuan Wu, Aijun Tian, Jiarui Xu, Qingjian Fang, Huiqin Huang, Yonghua Hu
    Aquaculture.2024; 582: 740528.     CrossRef
  • For Someone, You Are the Whole World: Host-Specificity of Salmonella enterica
    Anastasiya V. Merkushova, Anton E. Shikov, Anton A. Nizhnikov, Kirill S. Antonets
    International Journal of Molecular Sciences.2023; 24(18): 13670.     CrossRef
  • Edwardsiella piscicida YccA: A novel virulence factor essential to membrane integrity, mobility, host infection, and host immune response
    Mengru Jin, Jiaojiao He, Jun Li, Yonghua Hu, Dongmei Sun, Hanjie Gu
    Fish & Shellfish Immunology.2022; 126: 318.     CrossRef
  • FtsH is required for protein secretion homeostasis and full bacterial virulence in Edwardsiella piscicida
    Wei Wang, Jiatiao Jiang, Hao Chen, Yuanxing Zhang, Qin Liu
    Microbial Pathogenesis.2021; 161: 105194.     CrossRef
  • RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli
    Jaejin Lee, Dong-Ho Lee, Che Ok Jeon, Kangseok Lee
    Journal of Microbiology.2019; 57(10): 910.     CrossRef
  • The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli
    Minho Lee, Minju Joo, Minji Sim, Se-Hoon Sim, Hyun-Lee Kim, Jaejin Lee, Minkyung Ryu, Ji-Hyun Yeom, Yoonsoo Hahn, Nam-Chul Ha, Jang-Cheon Cho, Kangseok Lee
    Scientific Reports.2019;[Epub]     CrossRef
Taxonomic description and genome sequence of Halobacillus marinus sp. nov., a novel strain isolated from Chilika Lake, India
Ananta N. Panda , Samir Ranjan Mishra , Lopamudra Ray , Surajit Das , Gurdeep Rastogi , Tapan Kumar Adhya , Mrutyunjay Suar , Vishakha Raina
J. Microbiol. 2018;56(4):223-230.   Published online April 2, 2018
DOI: https://doi.org/10.1007/s12275-018-7387-x
  • 397 View
  • 0 Download
  • 6 Crossref
AbstractAbstract PDF
A moderately halophilic spore forming, motile, Gram-positive, rod-shaped bacterial strain designated as KGW1T was isolated from water sample of Chilika Lake and characterized taxonomically using polyphasic approach. The strain grew in the presence of 0–25% (w/v) NaCl in marine salt agar media, hydrolyzes casein, and gelatin and shows presence of alkaline proteases. The major cell wall menaquinone was MK7 and major cellular fatty acids were anteiso-C15:0 (44.89%), anteiso-C17:0 (6.18%), isoC15:0 (19.38%), and iso-C16:0 (7.39%). Several chemotaxonomic features conform the isolate be a member of genus Halobacillus. The isolate KGW1T contained A1γ meso-Dpm-direct type of peptidoglycan which is different from its phylogenetically closest neighbours. The 16S rRNA gene sequence based phylogenetic analysis also revealed the strain KGW1T was affiliated to the genus Halobacillus and sequence similarity between the isolated strain and the type strains of Halobacillus species were found closest to, H. dabanensis D-8 DSM 18199T (99.08%) and H. faecis IGA7-4 DSM 21559T (99.01%), H. trueperi SL-5 DSM 10404T (98.94%). The in silico DDH showed that the values in a range of 14.2–17.5% with the most closest strain H. dabanensis D-8 DSM 18199T and other type strains of the genus Halobacillus for which whole genome sequence is reported. DNA-DNA relatedness between strain KGW1T and the closest type strain Halobacillus trueperi DSM 10404T was 11.75% (± 1.15). The draft genome sequence includes 3,683,819 bases and comprises of 3898 predicted coding sequences with a G + C content of 46.98%. Thus, the significant distinctiveness supported by phenotypic and genotypic data with its closest neighbors and other closely related species confirm the strain KGW1T to be classified as a novel species within the genus Halobacillus, for which the name Halobacillus marinus sp. nov. is proposed. The type strain is KGW1T (= DSM 29522 = JCM 30443).

Citations

Citations to this article as recorded by  
  • Trachyspermum ammi seed extract-mediated Ag nanoparticles: an insight into its in vitro biopotency
    Vikneshvar K. S., R Subashini, Anieya Israel, Karuvelan Murugan, Namitha Ramakrishnan
    Biomass Conversion and Biorefinery.2025; 15(1): 313.     CrossRef
  • Halobacillus as source of natural products and enzyme factories
    Andri Frediansyah, Dhea Sandra Fitriany
    Extremophiles.2025;[Epub]     CrossRef
  • A comprehensive study of novel extremophilic soil bacterial isolates from Sundarbans mangrove sediments as a biocontrol agent for mosquito vector management
    Souvik Bag, Soumendranath Chatterjee
    Pest Management Science.2025; 81(10): 7154.     CrossRef
  • Molecular mechanisms underlying salt tolerance and plant growth promotion in wheat regulated by Halobacillus marinus SL2 and Halomonas elongata DM6
    Kiran DINDHORIA, Ashif ALI, Ayush LEPCHA, Rakshak KUMAR
    Pedosphere.2025;[Epub]     CrossRef
  • Draft genome sequence of Halobacillus campisalis strain ASL-17
    Anushree Srivastava, Michael Christopher Macey, Terry J. McGenity, Karen Olsson-Francis, Frank J. Stewart
    Microbiology Resource Announcements.2024;[Epub]     CrossRef
  • Identification of antibacterial metabolites produced by a marine bacterium Halobacillus marinus HMALI004
    Sardar Ali, Runlin Cai, Hao Feng, Jianmin Xie, Yueling Zhang, Hui Wang
    Journal of Applied Microbiology.2022; 133(5): 3030.     CrossRef
A common evolutionary pathway for maintaining quorum sensing in Pseudomonas aeruginosa
Bai-min Lai , Hui-cong Yan , Mei-zhen Wang , Na Li , Dong-sheng Shen
J. Microbiol. 2018;56(2):83-89.   Published online February 2, 2018
DOI: https://doi.org/10.1007/s12275-018-7286-1
  • 362 View
  • 0 Download
  • 12 Crossref
AbstractAbstract PDF
In the bacterium Pseudomonas aeruginosa, the synthesis and secretion of extracellular protease is a typical cooperative behavior regulated by quorum sensing. However, this type of cooperative behavior is easily exploited by other individuals who do not synthesize public goods, which is known as the “tragedy of the commons”. Here P. aeruginosa was inoculated into casein media with different nitrogen salts added. In casein broth, protease (a type of public good) is necessary for bacterial growth. After 30 days of sequential transfer, some groups propagated stably and avoided “tragedy of the commons”. The evolved cooperators who continued to synthesize protease were isolated from these stable groups. By comparing the characteristics of quorum sensing in these cooperators, an identical evolutionary pattern was found. A variety of cooperative behaviors regulated by quorum sensing, such as the synthesis and secretion of protease and signals, were significantly reduced during the process of evolution. Such reductions improved the efficiency of cooperation, helping to prevent cheating. In addition, the production of pyocyanin, which is regulated by the RhlIR system, increased during the process of evolution, possibly due to its role in stabilizing the cooperation. This study contributes towards our understanding of the evolution of quorum sensing of P. aeruginosa.

Citations

Citations to this article as recorded by  
  • Role of horizontal gene transfer and cooperation in rhizosphere microbiome assembly
    Simone Raposo Cotta, Armando Cavalcante Franco Dias, Rodrigo Mendes, Fernando Dini Andreote
    Brazilian Journal of Microbiology.2025; 56(1): 225.     CrossRef
  • Challenging the paradigm: non-canonical exoprotease cheating in clinical Pseudomonas aeruginosa isolates
    Katya Dafne Guadarrama-Orozco, Diego Armando Esquivel-Hernández, Miguel Ángel Islas-Tolentino, Fohad Mabood Husain, Héctor Quezada, Selene García-Reyes, Bernardo Franco, Diana Laura Marroquin-Mendiola, María Guadalupe Lucero-Gil, Lorena Paola Olvera-Falfa
    FEMS Microbiology Ecology.2025;[Epub]     CrossRef
  • Diesel degradation capability and environmental robustness of strain Pseudomonas aeruginosa WS02
    Penghong Luo, Yankui Tang, Jiahua Lu, Lu Jiang, Yiting Huang, Qiming Jiang, Xuemin Chen, Tianfu Qin, Holly Alice Shiels
    Journal of Environmental Management.2024; 351: 119937.     CrossRef
  • Biofilm control on metallic materials in medical fields from the viewpoint of materials science – from the fundamental aspects to evaluation
    Hideyuki Kanematsu, Dana M. Barry, Hajime Ikegai, Yoshimitsu Mizunoe
    International Materials Reviews.2023; 68(3): 247.     CrossRef
  • To cheat or not to cheat: cheatable and non-cheatable virulence factors in Pseudomonas aeruginosa
    Katya Dafne Guadarrama-Orozco, Caleb Perez-Gonzalez, Kokila Kota, Miguel Cocotl-Yañez, Jesús Guillermo Jiménez-Cortés, Miguel Díaz-Guerrero, Mariel Hernández-Garnica, Julia Munson, Frederic Cadet, Luis Esaú López-Jácome, Ángel Yahir Estrada-Velasco, Ana M
    FEMS Microbiology Ecology.2023;[Epub]     CrossRef
  • Exoprotease exploitation and social cheating in a Pseudomonas aeruginosa environmental lysogenic strain with a noncanonical quorum sensing system
    Daniel Huelgas-Méndez, Daniel Cazares, Luis David Alcaraz, Corina Diana Ceapã, Miguel Cocotl-Yañez, Toya Shotaro, Toshinari Maeda, Ana María Fernández-Presas, Oswaldo Tostado-Islas, Ana Lorena González-Vadillo, Aldo Limones-Martínez, Carlos Eduardo Hernan
    FEMS Microbiology Ecology.2023;[Epub]     CrossRef
  • 3-Phenylpropan-1-Amine Enhanced Susceptibility of Serratia marcescens to Ofloxacin by Occluding Quorum Sensing
    Lujun Yin, Ping-Ping Zhang, Wei Wang, Shi Tang, Shi-Ming Deng, Ai-Qun Jia, Gyanu Lamichhane
    Microbiology Spectrum.2022;[Epub]     CrossRef
  • A deep insight into the suppression mechanism of Sedum alfredii root exudates on Pseudomonas aeruginosa based on quorum sensing
    Min Zhu, Yusheng Yang, Meizhen Wang, Xiaoxiao Li, Ruifang Han, Qianqian Chen, Dongsheng Shen, Jiali Shentu
    Ecotoxicology and Environmental Safety.2021; 217: 112240.     CrossRef
  • Tobramycin Adaptation Enhances Policing of Social Cheaters in Pseudomonas aeruginosa
    Rhea G. Abisado, John H. Kimbrough, Brielle M. McKee, Vaughn D. Craddock, Nicole E. Smalley, Ajai A. Dandekar, Josephine R. Chandler, Rebecca E. Parales
    Applied and Environmental Microbiology.2021;[Epub]     CrossRef
  • Quercus infectoria gall extracts reduce quorum sensing-controlled virulence factors production and biofilm formation in Pseudomonas aeruginosa recovered from burn wounds
    Akhter Ahmed Ahmed, Fraidoon Abdulqadir Salih
    BMC Complementary and Alternative Medicine.2019;[Epub]     CrossRef
  • Seeding Public Goods Is Essential for Maintaining Cooperation in Pseudomonas aeruginosa
    Daniel Loarca, Dánae Díaz, Héctor Quezada, Ana Laura Guzmán-Ortiz, Abril Rebollar-Ruiz, Ana María Fernández Presas, Jimena Ramírez-Peris, Rafael Franco-Cendejas, Toshinari Maeda, Thomas K. Wood, Rodolfo García-Contreras
    Frontiers in Microbiology.2019;[Epub]     CrossRef
  • Pyocyanin Restricts Social Cheating in Pseudomonas aeruginosa
    Paulina Castañeda-Tamez, Jimena Ramírez-Peris, Judith Pérez-Velázquez, Christina Kuttler, Ammar Jalalimanesh, Miguel Á. Saucedo-Mora, J. Guillermo Jiménez-Cortés, Toshinari Maeda, Yael González, María Tomás, Thomas K. Wood, Rodolfo García-Contreras
    Frontiers in Microbiology.2018;[Epub]     CrossRef
Identification of essential genes of Pseudomonas aeruginosa for its growth in airway mucus
Mohammed Abd Alrahman , Sang Sun Yoon
J. Microbiol. 2017;55(1):68-74.   Published online December 30, 2016
DOI: https://doi.org/10.1007/s12275-017-6515-3
  • 361 View
  • 2 Download
  • 8 Crossref
AbstractAbstract PDF
Pseudomonas aeruginosa has been identified as an important causative agent of airway infection, mainly in cystic fibrosis. This disease is characterized by defective mucociliary clearance induced in part by mucus hyper-production. Mucin is a major component of airway mucus and is heavily O-glycosylated, with a protein backbone. Airway infection is known to be established with bacterial adhesion to mucin. However, the genes involved in mucin degradation or utilization remain elusive. In this study, we sought to provide a genetic basis of P. aeruginosa airway growth by identifying those genes. First, using RNASeq analyses, we compared genome-wide expression profiles of PAO1, a prototype P. aeruginosa laboratory strain, grown in M9-mucin (M9M) and M9-glucose (M9G) media. Additionally, a PAO1 transposon (Tn) insertion mutants library was screened for mutants defective in growth in M9M medium. One mutant with a Tn insertion in the xcpU gene (PA3100) was determined to exhibit faulty growth in M9M medium. This gene contributes to the type II secretion system, suggesting that P. aeruginosa uses this secretion system to produce a number of proteins to break down and assimilate the mucin molecule. Furthermore, we screened the PAO1 genome for genes with protease activity. Of 13 mutants, one with mutation in PA3247 gene exhibited defective growth in M9M, suggesting that the PA3247-encoded protease plays a role in mucin utilization. Further mechanistic dissection of this particular process will reveal new drug targets, the inhibition of which could control recalcitrant P. aeruginosa infections.

Citations

Citations to this article as recorded by  
  • Citrobacter rodentium possesses a functional type II secretion system necessary for successful host infection
    Z Krekhno, SE Woodward, A Serapio-Palacios, J Peña-Díaz, KM Moon, LJ Foster, BB Finlay
    Gut Microbes.2024;[Epub]     CrossRef
  • Cross-talk between cancer and Pseudomonas aeruginosa mediates tumor suppression
    Juliana K. Choi, Samer A. Naffouje, Masahide Goto, Jing Wang, Konstantin Christov, David J. Rademacher, Albert Green, Arlene A. Stecenko, Ananda M. Chakrabarty, Tapas K. Das Gupta, Tohru Yamada
    Communications Biology.2023;[Epub]     CrossRef
  • Pseudomonas aeruginosa type IV pili actively induce mucus contraction to form biofilms in tissue-engineered human airways
    Tamara Rossy, Tania Distler, Lucas A. Meirelles, Joern Pezoldt, Jaemin Kim, Lorenzo Talà, Nikolaos Bouklas, Bart Deplancke, Alexandre Persat, Victor Sourjik
    PLOS Biology.2023; 21(8): e3002209.     CrossRef
  • Impact of diet and the bacterial microbiome on the mucous barrier and immune disorders
    Charlotte A. Alemao, Kurtis F. Budden, Henry M. Gomez, Saima F. Rehman, Jacqueline E. Marshall, Shakti D. Shukla, Chantal Donovan, Samuel C. Forster, Ian A. Yang, Simon Keely, Elizabeth R. Mann, Emad M. El Omar, Gabrielle T. Belz, Philip M. Hansbro
    Allergy.2021; 76(3): 714.     CrossRef
  • The Bactericidal Tandem Drug, AB569: How to Eradicate Antibiotic-Resistant Biofilm Pseudomonas aeruginosa in Multiple Disease Settings Including Cystic Fibrosis, Burns/Wounds and Urinary Tract Infections
    Daniel J. Hassett, Rhett A. Kovall, Michael J. Schurr, Nalinikanth Kotagiri, Harshita Kumari, Latha Satish
    Frontiers in Microbiology.2021;[Epub]     CrossRef
  • Structural and functional analysis of the carotenoid biosynthesis genes of aPseudomonasstrain isolated from the excrement of Autumn Darter
    Yuki Fukaya, Miho Takemura, Takashi Koyanagi, Takashi Maoka, Kazutoshi Shindo, Norihiko Misawa
    Bioscience, Biotechnology, and Biochemistry.2018; 82(6): 1043.     CrossRef
  • Evolutionary conservation of the antimicrobial function of mucus: a first defence against infection
    Cassie R Bakshani, Ana L Morales-Garcia, Mike Althaus, Matthew D Wilcox, Jeffrey P Pearson, John C Bythell, J Grant Burgess
    npj Biofilms and Microbiomes.2018;[Epub]     CrossRef
  • Expanding Role of Type II Secretion in Bacterial Pathogenesis and Beyond
    Nicholas P. Cianciotto, Richard C. White, Anthony T. Maurelli
    Infection and Immunity.2017;[Epub]     CrossRef
Diversity and enzyme activity of Penicillium species associated with macroalgae in Jeju Island
Myung Soo Park , Seobihn Lee , Seung-Yoon Oh , Ga Youn Cho , Young Woon Lim
J. Microbiol. 2016;54(10):646-654.   Published online September 30, 2016
DOI: https://doi.org/10.1007/s12275-016-6324-0
  • 463 View
  • 1 Download
  • 18 Crossref
AbstractAbstract PDF
A total of 28 strains of 19 Penicillium species were isolated in a survey of extracellular enzyme-producing fungi from macroalgae along the coast of Jeju Island of Korea. Penicillium species were identified based on morphological and β-tubulin sequence analyses. In addition, the halo-tolerance and enzyme activity of all strains were evaluated. The diversity of Penicillium strains isolated from brown algae was higher than the diversity of strains isolated from green and red algae. The commonly isolated species were Penicillium antarcticum, P. bialowiezense, P. brevicompactum, P. crustosum, P. oxalicum, P. rubens, P. sumatrense, and P. terrigenum. While many strains showed endoglucanase, β-glucosidase, and protease activity, no alginase activity was detected. There was a positive correlation between halo-tolerance and endoglucanase activity within Penicillium species. Among 19 Penicillium species, three species–P. kongii, P. olsonii, and P. viticola– have not been previously recorded in Korea.

Citations

Citations to this article as recorded by  
  • Bioencapsulation of Hesperidinase from Penicillium sp. Toward Biocompounds with Enhanced Bioactivity
    Diogo F. Ribeiro, Ana Catarina Severo, Maria H. L. Ribeiro
    Compounds.2025; 5(2): 12.     CrossRef
  • Expanding the Inventory of Seven Unrecorded Marine Penicillium with Morphological Descriptions and Phenotypic Variability
    Wonjun Lee, Ji Seon Kim, Sumin Jo, Young Woon Lim
    Mycobiology.2025; 53(5): 648.     CrossRef
  • Plastic-inhabiting fungi in marine environments and PCL degradation activity
    Sung Hyun Kim, Jun Won Lee, Ji Seon Kim, Wonjun Lee, Myung Soo Park, Young Woon Lim
    Antonie van Leeuwenhoek.2022; 115(12): 1379.     CrossRef
  • Marine fungal abilities to enzymatically degrade algal polysaccharides, proteins and lipids: a review
    Yoran Le Strat, Nicolas Ruiz, Joël Fleurence, Yves-François Pouchus, Paul Déléris, Justine Dumay
    Journal of Applied Phycology.2022; 34(3): 1131.     CrossRef
  • Characterization of two 1,3-β-glucan-modifying enzymes from Penicillium sumatraense reveals new insights into 1,3-β-glucan metabolism of fungal saprotrophs
    Valentina Scafati, Francesca Troilo, Sara Ponziani, Moira Giovannoni, Anna Scortica, Daniela Pontiggia, Francesco Angelucci, Adele Di Matteo, Benedetta Mattei, Manuel Benedetti
    Biotechnology for Biofuels and Bioproducts.2022;[Epub]     CrossRef
  • Four Unrecorded Aspergillus Species from the Rhizosphere Soil in South Korea
    Jun Won Lee, Sung Hyun Kim, Young-Hyun You, Young Woon Lim, Myung Soo Park
    Mycobiology.2021; 49(4): 346.     CrossRef
  • Advances in research on calf rennet substitutes and their effects on cheese quality
    Xiaofeng Liu, Yuanfeng Wu, Rongfa Guan, Guochao Jia, YuChen Ma, Yao Zhang
    Food Research International.2021; 149: 110704.     CrossRef
  • Mutation, Chemoprofiling, Dereplication, and Isolation of Natural Products from Penicillium oxalicum
    Vidushi Abrol, Manoj Kushwaha, Divya Arora, Sharada Mallubhotla, Sundeep Jaglan
    ACS Omega.2021; 6(25): 16266.     CrossRef
  • Evaluating the xerophilic potential of moulds on selected egg tempera paints on glass and wooden supports using fluorescent microscopy
    Janez Kosel, Maša Kavčič, Lea Legan, Klara Retko, Polonca Ropret
    Journal of Cultural Heritage.2021; 52: 44.     CrossRef
  • Dietary effects on gut microbiota of the mesquite lizard Sceloporus grammicus (Wiegmann, 1828) across different altitudes
    Nina Montoya-Ciriaco, Selene Gómez-Acata, Ligia Catalina Muñoz-Arenas, Luc Dendooven, Arturo Estrada-Torres, Aníbal H. Díaz de la Vega-Pérez, Yendi E. Navarro-Noya
    Microbiome.2020;[Epub]     CrossRef
  • Penicillium from Rhizosphere Soil in Terrestrial and Coastal Environments in South Korea
    Myung Soo Park, Jun Won Lee, Sung Hyun Kim, Ji-Hyun Park, Young-Hyun You, Young Woon Lim
    Mycobiology.2020; 48(6): 431.     CrossRef
  • Three Unrecorded Species Belonging toPenicilliumSectionSclerotiorafrom Marine Environments in Korea
    Myung Soo Park, Dawoon Chung, Kyunghwa Baek, Young Woon Lim
    Mycobiology.2019; 47(2): 165.     CrossRef
  • Fungal Diversity and Enzyme Activity Associated with the Macroalgae, Agarum clathratum
    Seobihn Lee, Myung Soo Park, Hanbyul Lee, Jae-Jin Kim, John A. Eimes, Young Woon Lim
    Mycobiology.2019; 47(1): 50.     CrossRef
  • Biodiversity of Penicillium species from marine environments in Portugal and description of Penicillium lusitanum sp. nov., a novel species isolated from sea water
    Micael F. M. Gonçalves, Liliana Santos, Bruno M. V. Silva, Alberto C. Abreu, Tânia F. L. Vicente, Ana C. Esteves, Artur Alves
    International Journal of Systematic and Evolutionary Microbiology.2019; 69(10): 3014.     CrossRef
  • Taxonomic revision of the biotechnologically important species Penicillium oxalicum with the description of two new species from acidic and saline soils
    Alena Kubátová, Martina Hujslová, Jens C. Frisvad, Milada Chudíčková, Miroslav Kolařík
    Mycological Progress.2019; 18(1-2): 215.     CrossRef
  • The diversity and ecological roles of Penicillium in intertidal zones
    Myung Soo Park, Seung-Yoon Oh, Jonathan J. Fong, Jos Houbraken, Young Woon Lim
    Scientific Reports.2019;[Epub]     CrossRef
  • Fungal Root Microbiome from Healthy and Brittle Leaf Diseased Date Palm Trees (Phoenix dactylifera L.) Reveals a Hidden Untapped Arsenal of Antibacterial and Broad Spectrum Antifungal Secondary Metabolites
    Fedia B. Mefteh, Amal Daoud, Ali Chenari Bouket, Faizah N. Alenezi, Lenka Luptakova, Mostafa E. Rateb, Adel Kadri, Neji Gharsallah, Lassaad Belbahri
    Frontiers in Microbiology.2017;[Epub]     CrossRef
  • Species List of Aspergillus, Penicillium and Talaromyces in Korea, Based on ‘One Fungus One Name’ System

    The Korean Journal of Mycology.2016;[Epub]     CrossRef
Research Support, Non-U.S. Gov'ts
Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules
Young Jun An , Jung-Hyun Na , Myung-Il Kim , Sun-Shin Cha
J. Microbiol. 2015;53(10):711-717.   Published online October 2, 2015
DOI: https://doi.org/10.1007/s12275-015-5417-5
  • 370 View
  • 0 Download
  • 3 Crossref
AbstractAbstract
Lon proteases degrade defective or denature proteins as well as some folded proteins for the control of cellular protein quality. There are two types of Lon proteases, LonA and LonB. Each consists of two functional components: a protease component and an ATPase associated with various cellular activities (AAA+ module). Here, we report the 2.03 Å-resolution crystal structure of the isolated AAA+ module (iAAA+ module) of LonB from Thermococcus onnurineus NA1 (TonLonB). The iAAA+ module, having no bound nucleotide, adopts a conformation virtually identical to the ADP-bound conformation of AAA+ modules in the hexameric structure of TonLonB; this provides insights into the ATP-independent proteolytic activity observed in a LonB protease. Structural comparison of AAA+ modules between LonA and LonB revealed that the AAA+ modules of Lon proteases are separated into two distinct clades depending on their structural features. The AAA+ module of LonB belongs to the ‘H2 & Ins1 insert clade (HINS clade)’ defined for the first time in this study, while the AAA+ module of LonA is a member of the HCLR clade.

Citations

Citations to this article as recorded by  
  • Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases
    Alla Gustchina, Mi Li, Anna G. Andrianova, Arsen M. Kudzhaev, George T. Lountos, Bartosz Sekula, Scott Cherry, Joseph E. Tropea, Ivan V. Smirnov, Alexander Wlodawer, Tatyana V. Rotanova
    International Journal of Molecular Sciences.2022; 23(19): 11425.     CrossRef
  • Structure and the Mode of Activity of Lon Proteases from Diverse Organisms
    Alexander Wlodawer, Bartosz Sekula, Alla Gustchina, Tatyana V. Rotanova
    Journal of Molecular Biology.2022; 434(7): 167504.     CrossRef
  • Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme
    Nicholas P. Robinson, Julie A. Maupin-Furlow
    Emerging Topics in Life Sciences.2018; 2(4): 561.     CrossRef
VvpM, an Extracellular Metalloprotease of Vibrio vulnificus, Induces Apoptotic Death of Human Cells
Mi-Ae Lee , Jeong-A Kim , Yu Jin Yang , Mee-Young Shin , Soon-Jung Park , Kyu-Ho Lee
J. Microbiol. 2014;52(12):1036-1043.   Published online November 3, 2014
DOI: https://doi.org/10.1007/s12275-014-4531-0
  • 449 View
  • 0 Download
  • 16 Crossref
AbstractAbstract PDF
A pathogenic bacterium, Vibrio vulnificus produces various extracellular proteases including the elastolytic metalloprotease, VvpE. In silico analysis of its genome revealed a VvpEhomologous protease, VvpM whose proteolytic activity was abolished by specific inhibitors against metalloproteases. To investigate whether this newly identified protease has pathogenic role in host interaction in addition to proteolytic role, human cell lines were incubated with recombinant VvpM (rVvpM). rVvpM-challenged cells showed typical morphological changes found in cells under apoptosis. Apoptotic cell death was further evidenced by estimating the Annexin V-stained cells, whose proportions were dependent upon the concentrations of rVvpM treated to human cells. To elucidate the signaling pathway for VvpM-induced apoptosis, three MAPKs were tested if their activation were mediated by rVvpM. ERK1/2 was phosphorylated by treatment of rVvpM and rVvpM-induced cell death was blocked by a specific inhibitor against ERK1/2. In rVvpM-treated cells, the cytosolic levels of cytochrome c were increased in a VvpM concentration- dependent manner, while the levels of cytochrome c in mitochondria were decreased. Cell deaths were accompanied by apparent cleavages of procaspases-9 and -3 to the active caspases-9 and -3, respectively. Therefore, this study demonstrates that an extracellular metalloprotease of V. vulnificus, VvpM induces apoptosis of human cells via a pathway consisting of ERK activation, cytochrome c release, and then activation of caspases-9 and -3.

Citations

Citations to this article as recorded by  
  • Pathology and pathogenesis of Vibrio infection in fish: A review
    Tilusha Manchanayake, Annas Salleh, Mohammad Noor Azmai Amal, Ina Salwany Md Yasin, Mohd Zamri-Saad
    Aquaculture Reports.2023; 28: 101459.     CrossRef
  • Direct and indirect effects of pathogenic bacteria on the integrity of intestinal barrier
    Lin-Zhen Shu, Yi-Dan Ding, Qing-Ming Xue, Wei Cai, Huan Deng
    Therapeutic Advances in Gastroenterology.2023;[Epub]     CrossRef
  • Vibrio vulnificus PlpA facilitates necrotic host cell death induced by the pore forming MARTX toxin
    Changyi Cho, Sanghyeon Choi, Myung Hee Kim, Byoung Sik Kim
    Journal of Microbiology.2022; 60(2): 224.     CrossRef
  • The DNA binding domain of theVibrio vulnificusSmcR transcription factor is flexible and binds diverse DNA sequences
    Jane D Newman, Meghan M Russell, Lixin Fan, Yun-Xing Wang, Giovanni Gonzalez-Gutierrez, Julia C van Kessel
    Nucleic Acids Research.2021; 49(10): 5967.     CrossRef
  • Melatonin restores Muc2 depletion induced by V. vulnificus VvpM via melatonin receptor 2 coupling with Gαq
    Young-Min Lee, Jong Pil Park, Young Hyun Jung, Hyun Jik Lee, Jun Sung Kim, Gee Euhn Choi, Ho Jae Han, Sei-Jung Lee
    Journal of Biomedical Science.2020;[Epub]     CrossRef
  • The role of Vibrio vulnificus virulence factors and regulators in its infection-induced sepsis
    Gang Li, Ming-Yi Wang
    Folia Microbiologica.2020; 65(2): 265.     CrossRef
  • Intestinal epithelial cell apoptosis due to a hemolytic toxin from Vibrio vulnificus and protection by a 36 kDa glycoprotein from Rhus verniciflua Stokes
    Young-Min Lee, Jong Pil Park, Kye-Taek Lim, Sei-Jung Lee
    Food and Chemical Toxicology.2019; 125: 46.     CrossRef
  • The extracellular proteases produced by Vibrio parahaemolyticus
    George Osei-Adjei, Xinxiang Huang, Yiquan Zhang
    World Journal of Microbiology and Biotechnology.2018;[Epub]     CrossRef
  • Repression of VvpM Protease Expression by Quorum Sensing and the cAMP-cAMP Receptor Protein Complex in Vibrio vulnificus
    Jeong-A Kim, Mi-Ae Lee, You-Chul Jung, Bo-Ram Jang, Kyu-Ho Lee, Victor J. DiRita
    Journal of Bacteriology.2018;[Epub]     CrossRef
  • Classification and structural insight into vibriolysin-like proteases of Vibrio pathogenicity
    JiaFeng Huang, BingQi Zeng, Dan Liu, RiBang Wu, Jiang Zhang, BinQiang Liao, HaiLun He, Fei Bian
    Microbial Pathogenesis.2018; 117: 335.     CrossRef
  • A Vibrio vulnificus VvpM Induces IL-1β Production Coupled with Necrotic Macrophage Death via Distinct Spatial Targeting by ANXA2
    Sei-Jung Lee, Young Hyun Jung, Jun Sung Kim, Hyun Jik Lee, Sang Hun Lee, Kyu-Ho Lee, Kyung Ku Jang, Sang Ho Choi, Ho Jae Han
    Frontiers in Cellular and Infection Microbiology.2017;[Epub]     CrossRef
  • Vibrio vulnificus: An Environmental and Clinical Burden
    Sing-Peng Heng, Vengadesh Letchumanan, Chuan-Yan Deng, Nurul-Syakima Ab Mutalib, Tahir M. Khan, Lay-Hong Chuah, Kok-Gan Chan, Bey-Hing Goh, Priyia Pusparajah, Learn-Han Lee
    Frontiers in Microbiology.2017;[Epub]     CrossRef
  • Crystal Structure of the Regulatory Domain of AphB from Vibrio vulnificus, a Virulence Gene Regulator
    Nohra Park, Saemee Song, Garam Choi, Kyung Ku Jang, Inseong Jo, Sang Ho Choi, Nam-Chul Ha
    Molecules and Cells.2017; 40(4): 299.     CrossRef
  • The hydrogen peroxide hypersensitivity of OxyR2 in Vibrio vulnificus depends on conformational constraints
    Inseong Jo, Dukyun Kim, Ye-Ji Bang, Jinsook Ahn, Sang Ho Choi, Nam-Chul Ha
    Journal of Biological Chemistry.2017; 292(17): 7223.     CrossRef
  • The Makes Caterpillars Floppy (MCF)-Like Domain of Vibrio vulnificus Induces Mitochondrion-Mediated Apoptosis
    Shivangi Agarwal, Yeuming Zhu, David R. Gius, Karla J. F. Satchell, S. M. Payne
    Infection and Immunity.2015; 83(11): 4392.     CrossRef
  • Stationary‐phase induction of vvpS expression by three transcription factors: repression by LeuO and activation by SmcR and CRP
    Jeong‐A. Kim, Jin Hwan Park, Mi‐Ae Lee, Hyun‐Jung Lee, Soon‐Jung Park, Kun‐Soo Kim, Sang‐Ho Choi, Kyu‐Ho Lee
    Molecular Microbiology.2015; 97(2): 330.     CrossRef
Identification of Proteolytic Bacteria from the Arctic Chukchi Sea Expedition Cruise and Characterization of Cold-active Proteases
Ha Ju Park , Yung Mi Lee , Sunghui Kim , Ah Ram Wi , Se Jong Han , Han-Woo Kim , Il-Chan Kim , Joung Han Yim , Dockyu Kim
J. Microbiol. 2014;52(10):825-833.   Published online August 27, 2014
DOI: https://doi.org/10.1007/s12275-014-4226-6
  • 440 View
  • 0 Download
  • 9 Crossref
AbstractAbstract PDF
Following collection of seawater samples during an Arctic Chukchi Sea expedition cruise of the Korean icebreaker Araon in 2012, a total of 15,696 bacteria were randomly isolated from Marine Broth 2216 agar plates. Of these, 2,526 (16%) showed proteolytic activity and were identified as mainly Alteromonas (31%), Staphylococcus (27%), and Pseudoalteromonas (14%). Among the proteolytic strains, seven were selected based on their significant ability to grow and produce a halo on skim milk plates at low temperatures (<5°C) owing to cold-active proteases. These strains were affiliated with the genus Pseudoalteromonas and were divided into three groups based on phylogenetic analysis of the 16S rRNA genes. Profiling cell membrane fatty acids confirmed the 16S rRNA-based differentiation and revealed the accordance between the two analyses. Seven genes for serine protease precursors were amplified from the corresponding strains, and based on sequence similarities, these genes were divided into three groups that were identical to those identified by the 16S rRNA phylogenetic analysis. Three protease genes from the representative strains of each group were composed of 2,127–2,130 bp, encoding 708–709 amino acids, and these genes yielded products with calculated molecular weights of approximately 72.3–72.8 kDa. Amino acid sequence analysis suggested that the precursors are members of the subtilase serine endo- and exo-peptidase clan and contain four domains (signal peptide, N-terminal prosequence, catalytic domain, and two pre-peptidase C-terminal domains). Upon expression in E. coli, each recombinant protease exhibited proteolytic activity on zymogram gels.

Citations

Citations to this article as recorded by  
  • The Arctic summer microbiome across Fram Strait: Depth, longitude, and substrate concentrations structure microbial diversity in the euphotic zone
    Matthias Wietz, Anja Engel, Simon Ramondenc, Matomo Niwano, Wilken‐Jon von Appen, Taylor Priest, Anabel von Jackowski, Katja Metfies, Christina Bienhold, Antje Boetius
    Environmental Microbiology.2024;[Epub]     CrossRef
  • Diversity in the utilization of different molecular classes of dissolved organic matter by heterotrophic marine bacteria
    Shira Givati, Elena Forchielli, Dikla Aharonovich, Noga Barak, Osnat Weissberg, Natalia Belkin, Eyal Rahav, Daniel Segrè, Daniel Sher, Jennifer F. Biddle
    Applied and Environmental Microbiology.2024;[Epub]     CrossRef
  • Benthic bacteria and archaea in the North American Arctic reflect food supply regimes and impacts of coastal and riverine inputs
    Alexis M. Walker, Mary Beth Leigh, Sarah L. Mincks
    Deep Sea Research Part II: Topical Studies in Oceanography.2023; 207: 105224.     CrossRef
  • Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst
    Zhengfeng Yang, Zhendi Huang, Qian Wu, Xianghua Tang, Zunxi Huang
    International Journal of Molecular Sciences.2023; 24(10): 8532.     CrossRef
  • Description of Polaribacter batillariae sp. nov., Polaribacter cellanae sp. nov., and Polaribacter pectinis sp. nov., novel bacteria isolated from the gut of three types of South Korean shellfish
    Su-Won Jeong, Jeong Eun Han, June-Young Lee, Ji-Ho Yoo, Do-Yeon Kim, In Chul Jeong, Jee-Won Choi, Yun-Seok Jeong, Jae-Yun Lee, So-Yeon Lee, Euon Jung Tak, Hojun Sung, Hyun Sik Kim, Pil Soo Kim, Dong-Wook Hyun, Jin-Woo Bae
    Journal of Microbiology.2022; 60(6): 576.     CrossRef
  • Proteases from the marine bacteria in the genus Pseudoalteromonas: diversity, characteristics, ecological roles, and application potentials
    Xiu-Lan Chen, Yan Wang, Peng Wang, Yu-Zhong Zhang
    Marine Life Science & Technology.2020; 2(4): 309.     CrossRef
  • Characterization of balofloxacin-stressed proteomics and identification of balofloxacin-binding proteins pre-peptidase and integration host factor in Edwardsiella tarda
    Qi Wen, Xian-jie Liu, Wei-cong Zhu, Lu Li, Min-yi Li, Xuna-xian Peng, Hui Li
    Journal of Proteomics.2019; 205: 103413.     CrossRef
  • The Place for Enzymes and Biologically Active Peptides from Marine Organisms for Application in Industrial and Pharmaceutical Biotechnology
    Jean-Étienne R.L. Morlighem, Gandhi Radis-Baptista
    Current Protein & Peptide Science.2019; 20(4): 334.     CrossRef
  • Benefit from decline: the primary transcriptome of Alteromonas macleodii str. Te101 during Trichodesmium demise
    Shengwei Hou, Mario López-Pérez, Ulrike Pfreundt, Natalia Belkin, Kurt Stüber, Bruno Huettel, Richard Reinhardt, Ilana Berman-Frank, Francisco Rodriguez-Valera, Wolfgang R Hess
    The ISME Journal.2018; 12(4): 981.     CrossRef
Functional Analysis of a Subtilisin-like Serine Protease Gene from Biocontrol Fungus Trichoderma harzianum
Haijuan Fan , Zhihua Liu , Rongshu Zhang , Na Wang , Kai Dou , Gulijimila Mijiti , Guiping Diao , Zhiying Wang
J. Microbiol. 2014;52(2):129-138.   Published online February 1, 2014
DOI: https://doi.org/10.1007/s12275-014-3308-9
  • 401 View
  • 1 Download
  • 21 Crossref
AbstractAbstract PDF
The subtilisin-like serine protease gene ThSS45 has been cloned from Trichoderma harzianum ACCC30371. Its coding region is 1302 bp in length, encoding 433 amino acids, with a predicted protein molecular weight of 44.9 kDa and pI of 5.91. ThSS45 was shown by RT-qPCR analysis to be differentially transcribed in response to eight different treatments. The transcription of ThSS45 was up-regulated when grown in mineral medium, under carbon starvation, and nitrogen starvation, and in the presence of 1% root powder, 1% stem powder, and 1% leaf powder derived from Populus davidiana × P. bolleana (Shanxin poplar) aseptic seedlings. The highest increase in transcription approached 3.5-fold that of the control at 6 h under induction with 1% poplar root powder. The transcription of ThSS45 was also slightly up-regulated by 1% Alternaria alternata cell wall and 5% A. alternata fermentation liquid. Moreover, the analyses of coding and promoter regions of ThSS45 homologs indicated that serine protease may be involved in both mycoparasitism and antibiotic secretion. ThSS45 was cloned into the pGEX-4T-2 vector and then expressed in Escherichia coli BL21. The recombinant protein, with an expected molecular weight of approximately 69 kDa, was then purified. When transformant BL21-ss was induced with 1 mM IPTG for 6 h, the purified protease activity reached a peak of 18.25 U/ml at pH 7.0 and 40°C. In antifungal assays the purified protease obviously inhibited the growth of A. alternata mycelia.

Citations

Citations to this article as recorded by  
  • Performance of hydrolytic enzymes produced by Trichoderma in sustainable crop production: Current insights and future perspectives
    Muhammad Haikal Algifari, Dedat Prismantoro, Anggita Rahmi Hafsari, Mia Miranti, Wan Abd Al Qadr Imad Wan-Mohtar, Abdullah Bilal Ozturk, Azwir Anhar, Zul Ilham, Ravindra Chandra Joshi, Febri Doni
    Sustainable Environment.2025;[Epub]     CrossRef
  • The role of Trichoderma koningii and Trichoderma harzianum in mitigating the combined stresses motivated by Sclerotiniasclerotiorum and salinity in common bean (Phaseolusvulgaris)
    Abdelrazek S. Abdelrhim, Nada F. Hemeda, Mai Ali Mwaheb, Maha O.A. Omar, Mona F.A. Dawood
    Plant Stress.2024; 11: 100370.     CrossRef
  • Mechanism of oxalate decarboxylase Oxd_S12 from Bacillus velezensis BvZ45-1 in defence against cotton verticillium wilt
    Ying Sun, Na Yang, Sirui Li, Fei Chen, Yijing Xie, Canming Tang, Monica Höfte
    Journal of Experimental Botany.2024; 75(11): 3500.     CrossRef
  • Purification and Identification of the Nematicidal Activity of S1 Family Trypsin-Like Serine Protease (PRA1) from Trichoderma longibrachiatum T6 Through Prokaryotic Expression and Biological Function Assays
    Nan Ma, Hang Lv, Solomon Boamah, Shuwu Zhang, Bingliang Xu
    Genes.2024; 15(11): 1437.     CrossRef
  • Genome and transcriptome sequencing of Trichoderma harzianum T4, an important biocontrol fungus of Rhizoctonia solani, reveals genes related to mycoparasitism
    Yaping Wang, Jian Wang, Xiaochong Zhu, Wei Wang
    Canadian Journal of Microbiology.2024; 70(3): 86.     CrossRef
  • Strain improvement of Trichoderma harzianum for enhanced biocontrol capacity: Strategies and prospects
    Ziyang Xiao, Qinqin Zhao, Wei Li, Liwei Gao, Guodong Liu
    Frontiers in Microbiology.2023;[Epub]     CrossRef
  • Analysis of the Properties of 44 ABC Transporter Genes from Biocontrol Agent Trichoderma asperellum ACCC30536 and Their Responses to Pathogenic Alternaria alternata Toxin Stress
    Hua-Ying Du, Yu-Zhou Zhang, Kuo Liu, Pei-Wen Gu, Shuang Cao, Xiang Gao, Zhi-Ying Wang, Zhi-Hua Liu, Ze-Yang Yu
    Current Issues in Molecular Biology.2023; 45(2): 1570.     CrossRef
  • Insights into the ecological generalist lifestyle of Clonostachys fungi through analysis of their predicted secretomes
    Edoardo Piombo, Micol Guaschino, Dan Funck Jensen, Magnus Karlsson, Mukesh Dubey
    Frontiers in Microbiology.2023;[Epub]     CrossRef
  • The dark septate endophyte Phialocephala sphaeroides suppresses conifer pathogen transcripts and promotes root growth of Norway spruce
    Kai Wang, Zilan Wen, Fred O Asiegbu, Malin Elfstrand
    Tree Physiology.2022; 42(12): 2627.     CrossRef
  • Extracellular proteins of Trichoderma and their role in plant health
    Anu Sharma, Richa Salwan, Vivek Sharma
    South African Journal of Botany.2022; 147: 359.     CrossRef
  • Predicted Input of Uncultured Fungal Symbionts to a Lichen Symbiosis from Metagenome-Assembled Genomes
    Gulnara Tagirdzhanova, Paul Saary, Jeffrey P Tingley, David Díaz-Escandón, D Wade Abbott, Robert D Finn, Toby Spribille, Jason Stajich
    Genome Biology and Evolution.2021;[Epub]     CrossRef
  • Production of tailor-made enzymes to facilitate lipid extraction from the oleaginous yeast Schwanniomyces occidentalis
    Ruud Heshof, Bram Visscher, Eric van de Zilver, Rick van de Vondervoort, Femke van Keulen, Roy J. B. M. Delahaije, Richèle D. Wind
    AMB Express.2020;[Epub]     CrossRef
  • An approach to select Lactobacillus isolates as protective cultures for food fermentations
    Raffael C. Inglin, Alessia I. Delbrück, Benjamin Fässler, Katharina E. Siebenmann, Christophe Lacroix, Marc J. A. Stevens, Leo Meile
    Journal of Food Safety.2018;[Epub]     CrossRef
  • Biocontrol activity of recombinant aspartic protease from Trichoderma harzianum against pathogenic fungi
    Jun-Jin Deng, Wei-Qian Huang, Zhi-Wei Li, De-Lin Lu, Yuanyuan Zhang, Xiao-chun Luo
    Enzyme and Microbial Technology.2018; 112: 35.     CrossRef
  • Functional analysis of eliciting plant response protein Epl1-Tas from Trichoderma asperellum ACCC30536
    Wenjing Yu, Gulijimila Mijiti, Ying Huang, Haijuan Fan, Yucheng Wang, Zhihua Liu
    Scientific Reports.2018;[Epub]     CrossRef
  • Comparative evolutionary histories of fungal proteases reveal gene gains in the mycoparasitic and nematode-parasitic fungus Clonostachys rosea
    Mudassir Iqbal, Mukesh Dubey, Mikael Gudmundsson, Maria Viketoft, Dan Funck Jensen, Magnus Karlsson
    BMC Evolutionary Biology.2018;[Epub]     CrossRef
  • Expression analysis on mycoparasitism related genes during antagonism of Trichoderma with Colletotrichum falcatum causing red rot in sugarcane
    Elangovan Elamathi, Palaniyandi Malathi, Rasappa Viswanathan, Amalraj Ramesh Sundar
    Journal of Plant Biochemistry and Biotechnology.2018; 27(3): 351.     CrossRef
  • Subtilisin-like serine protease gene TghSS42 from Trichoderma ghanense ACCC 30153 was successfully expressed in Escherichia coli and recombinant protease rTghSS42 exhibited antifungal ability to five phytopathogens
    HUIFANG ZHANG, NA WANG, YUCHENG WANG, JINJIE WANG, HONG ZHENG, ZHIHUA LIU
    Biocontrol Science.2017; 22(3): 145.     CrossRef
  • A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101
    Maroua Omrane Benmrad, Emna Moujehed, Mouna Ben Elhoul, Nadia Zaraî Jaouadi, Sondes Mechri, Hatem Rekik, Sidali Kourdali, Mohamed El Hattab, Abdelmalek Badis, Sami Sayadi, Samir Bejar, Bassem Jaouadi
    International Journal of Biological Macromolecules.2016; 91: 961.     CrossRef
  • Differential Response of Extracellular Proteases of Trichoderma Harzianum Against Fungal Phytopathogens
    Vivek Sharma, Richa Salwan, Prem N. Sharma
    Current Microbiology.2016; 73(3): 419.     CrossRef
  • Fungal proteins and genes associated with biocontrol mechanisms of soil-borne pathogens: a review
    Yohann Daguerre, Katarzyna Siegel, Véronique Edel-Hermann, Christian Steinberg
    Fungal Biology Reviews.2014; 28(4): 97.     CrossRef
Identification and Characterization of an Anti-fungi Fusarium oxysporum f. sp. cucumerium Protease from the Bacillus subtilis Strain N7
Yi Luo , Lifei Sun , Zhen Zhu , Wei Ran , Qirong Shen
J. Microbiol. 2013;51(3):359-366.   Published online June 28, 2013
DOI: https://doi.org/10.1007/s12275-013-2627-6
  • 301 View
  • 3 Download
  • 12 Crossref
AbstractAbstract PDF
A newly discovered alkaline antifungal protease named P6 from Bacillus subtilis N7 was purified and partially characterized. B. subtilis N7 culture filtrates were purified by 30–60% (NH4)2SO4 precipitation, anion-exchange chromatography and gel filtration chromatography. Sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) revealed a single band of 41.38 kDa. Peptide sequence of protease P6 was determined using a 4800 Plus MALDI TOF/TOFTM Analyzer System. Self-Formed Adaptor PCR (SEFA-PCR) was used to amplify the 1,149 bp open read frame of P6. Dimensional structure prediction using Automatic Modeling Mode software showed that the protease P6 consisted of two β-barrel domains. Purified P6 strongly inhibited spore and mycelium growth of Fusarium oxysporum f. sp. cucumerium (FOC) by causing hypha lysis when the concentration was 25 μg/ml. Characterization of the purified protease indicated that it had substrate specificity for gelatin and was highly active at pH 8.0–10.6 and 70°C. The P6 protease was inhibited by EDTA (2 mmol/L), phenyl methyl sulfonyl fluoride (PMSF, 1 mmol/L), Na+, Fe3+, Cu2+, Mg2+ (5 mmol/L each) and H2O2 (2%, v/v). However, protease activity was activated by Ca2+, K+, Mn2+ (5 mmol/L each), mercaptoethanol (2%, v/v) and Tween 80 (1%, v/v). In additon, activity was also affected by organic solvents such as acetone, normal butanol and ethanol, but not hexane (25%, v/v each).

Citations

Citations to this article as recorded by  
  • Genomic and functional analysis of Pseudomonas protegens CS11 reveals multifaceted biocontrol mechanisms against Sclerotinia sclerotiorum via antifungal metabolites, root colonisation and plant defence induction in tomato
    Aida Nabila Rahim, Gwo Rong Wong, Kah Ooi Chua, Kausalyaa Kaliapan, Jennifer Ann Harikrishna, Siah Ying Tang, Bey Hing Goh, Purabi Mazumdar
    Microbiological Research.2026; 304: 128399.     CrossRef
  • Mechanisms of Surfactin from Bacillus subtilis SF1 against Fusarium foetens: A Novel Pathogen Inducing Potato Wilt
    Lin Liu, Xiaofan Jin, Xiuhua Lu, Lizhong Guo, Peiwei Lu, Hao Yu, Beibei Lv
    Journal of Fungi.2023; 9(3): 367.     CrossRef
  • The Extracellular Lipopeptides and Volatile Organic Compounds of Bacillus subtilis DHA41 Display Broad-Spectrum Antifungal Activity against Soil-Borne Phytopathogenic Fungi
    Dhabyan Mutar Kareem Al-Mutar, Muhammad Noman, Noor Salih Abduljaleel Alzawar, Hadi Hussein Qasim, Dayong Li, Fengming Song
    Journal of Fungi.2023; 9(8): 797.     CrossRef
  • An Overview of Proteases: Production, Downstream Processes and Industrial Applications
    Nathiele Contrera Gimenes, Edgar Silveira, Elias Basile Tambourgi
    Separation & Purification Reviews.2021; 50(3): 223.     CrossRef
  • Biocontrol of Orchid-pathogenic Mold,Phytophthora palmivora, by Antifungal Proteins fromPseudomonas aeruginosaRS1
    Rapeewan Sowanpreecha, Panan Rerngsamran
    Mycobiology.2018; 46(2): 129.     CrossRef
  • Microbial Flora Associated with the Halophyte–Salsola imbricate and Its Biotechnical Potential
    Fehmida Bibi, Gary A. Strobel, Muhammad I. Naseer, Muhammad Yasir, Ahmed A. Khalaf Al-Ghamdi, Esam I. Azhar
    Frontiers in Microbiology.2018;[Epub]     CrossRef
  • Diversity of indigenous endophytic bacteria associated with the roots of Chinese cabbage (Brassica campestris L.) cultivars and their antagonism towards pathogens
    Md. Azizul Haque, Han Dae Yun, Kye Man Cho
    Journal of Microbiology.2016; 54(5): 353.     CrossRef
  • Isolation and anti- Verticillium dahliae activity from Bacillus axarquiensis TUBP1 protein
    Hong Zeng, Rong Chen, Xiaoxia Luo, Jun Tian
    Process Biochemistry.2016; 51(10): 1691.     CrossRef
  • Effect of Two Biological Formulations Based onBacillus subtilisandPseudomonas fluorescenson Control ofDidymella applanata, the Causal Agent of Red Raspberry Cane Spur Blight
    Margarita Shternshis, Tatyana Shpatova, Anatoly Belyaev
    International Journal of Agronomy.2016; 2016: 1.     CrossRef
  • Cucumber Rhizosphere Microbial Community Response to Biocontrol Agent Bacillus subtilis B068150
    Lihua Li, Jincai Ma, A. Ibekwe, Qi Wang, Ching-Hong Yang
    Agriculture.2015; 6(1): 2.     CrossRef
  • Construction of a heterologous gene expression system in the banana rhizobacterium strain GW-3 and its colonization ability
    Yuguang Wang, Qiyu Xia, He Zhang, Xuehua Lu, Jianbo Sun, Xin Zhang
    World Journal of Microbiology and Biotechnology.2014; 30(3): 903.     CrossRef
  • A novel antifungal protein of Bacillus subtilis B25
    Zhiqiong Tan, Baoying Lin, Rongyi Zhang
    SpringerPlus.2013;[Epub]     CrossRef
Characterization, Cloning, and Heterologous Expression of a Subtilisin-Like Serine Protease Gene VlPr1 from Verticillium lecanii
Gang Yu , Jin-Liang Liu , Li-Qin Xie , Xue-Liang Wang , Shi-Hong Zhang , Hong-Yu Pan
J. Microbiol. 2012;50(6):939-946.   Published online December 30, 2012
DOI: https://doi.org/10.1007/s12275-012-2199-x
  • 231 View
  • 0 Download
  • 12 Scopus
AbstractAbstract PDF
The entomopathogenic fungus Verticillium lecanii is a wellknown biocontrol agent. V. lecanii produces subtilisin-like serine protease (Pr1), which is important in the biological control activity of some insect pests by degrading insect cuticles. In this study, a subtilisin-like serine protease gene VlPr1 was cloned from the fungus and the VlPr1 protein was expressed in Escherichia coli. The VlPr1 gene contains an open reading frame (ORF) interrupted by three short introns, and encodes a protein of 379 amino acids. Protein sequence analysis revealed high homology with subtilisin serine proteases. The molecular mass of the protease was 38 kDa, and the serine protease exhibited its maximal activity at 40°C and pH 9.0. Protease activity was also affected by Mg2+ and Ca2+ concentration. The protease showed inhibitory activity against several plant pathogens, especially towards Fusarium moniliforme.
Purification and Partial Characterization of a Detergent and Oxidizing Agent Stable Alkaline Protease from a Newly Isolated Bacillus subtilis VSG-4 of Tropical Soil
Sib Sankar Giri , V. Sukumaran , Shib Sankar Sen , M. Oviya , B. Nazeema Banu , Prasant Kumar Jena
J. Microbiol. 2011;49(3):455-461.   Published online June 30, 2011
DOI: https://doi.org/10.1007/s12275-011-0427-4
  • 347 View
  • 0 Download
  • 23 Crossref
AbstractAbstract PDF
An extracellular detergent tolerant protease producing strain VSG-4 was isolated from tropical soil sample and identified as Bacillus subtilis based on morphological, biochemical characteristics as well as 16S-rRNA gene sequencing. The VSG-4 protease was purified to homogeneity using ammonium sulphate precipitation, dialysis and sephadex G-200 gel permeation chromatography with a 17.4 purification fold. The purified enzyme was active and stable over a broad range of pH (8.0-11.0, optimum at 9.0) and temperature (40°C to 60°C, optimum at 50°C). The thermostability of the enzyme was significantly increased by the addition CaCl2. This enzyme was strongly inhibited by PMSF and DFP, suggesting that it belongs to the serine protease superfamily. The purified VSG-4 alkaline protease showed remarkable stability in anionic (5 mM SDS) and ionic (1% Trion X-100 and 1% Tween 80) detergents. It retained 97±2% and 83.6±1.1% of its initial activity after 1 h preincubation in the presence of 1% H2O2 and 1% sodium perborate, respectively. Furthermore, the purified enzyme showed excellent stability and compatibility with some commercial laundry detergents besides its stain removal capacity. Considering these promising properties, VSG-4 protease may find tremendous application in laundry detergent formulations.

Citations

Citations to this article as recorded by  
  • Partial purification and characterization of protease extracted from kinema
    Dambar Bahadur Khadka, Tikaram Pahadi, Sunil Aryal, Dhan Bahadur Karki
    Heliyon.2024; 10(5): e27173.     CrossRef
  • Production, Optimization and Partial Characterization of Alkaline Protease from Bacillus subtilis spp. subtilis NRRL B-3384 and B-3387
    Cengiz AKKALE
    Hittite Journal of Science and Engineering.2023; 10(2): 135.     CrossRef
  • Phenotypic characteristics, phylogenetic analysis and characterization of alkaline proteases of marine bacteria Geomicrobium halophilum, Oceanobacillus oncorhynchi, and Oceanobacillus khimchii
    Vikram H. Raval, Rupal H. Joshi, Hitarth B. Bhatt, Satya P. Singh
    Biologia.2022; 77(8): 2405.     CrossRef
  • Compatibility and Washing Performance of Compound Protease Detergent
    Wei Zhang, Jintao Wu, Jing Xiao, Mingyao Zhu, Haichuan Yang
    Applied Sciences.2021; 12(1): 150.     CrossRef
  • Fishmeal Wastewater as A Low-Cost Nitrogen Source for γ-Polyglutamic Acid Production Using Bacillus subtilis
    Chao Zhang, Dao-Ji Wu, Jie Jia, Hong-Qi Yang
    Waste and Biomass Valorization.2019; 10(4): 789.     CrossRef
  • Cloning, expression, purification and characterisation of serine alkaline protease from Bacillus subtilis RD7
    Yewande Suberu, Idowu Akande, Titilola Samuel, Adekunle Lawal, Ademola Olaniran
    Biocatalysis and Agricultural Biotechnology.2019; 20: 101264.     CrossRef
  • Alkaline serine protease from the new halotolerant alkaliphilic Salipaludibacillus agaradhaerens strain AK-R: purification and properties
    Abdelnasser S. S. Ibrahim, Yahya B. Elbadawi, Mohamed A. El-Tayeb, Khalid S. Al-maary, Dina Abdel Fattah Maany, Shebl Salah S. Ibrahim, Atif A. Elagib
    3 Biotech.2019;[Epub]     CrossRef
  • Purification and characterization of alkaline, thermostable and organic solvent stable protease from a mutant of Bacillus sp.
    Neha Thakur, Ajay Kumar, Abhishek Sharma, Tek Chand Bhalla, Dinesh Kumar
    Biocatalysis and Agricultural Biotechnology.2018; 16: 217.     CrossRef
  • Characterization of a robust serine protease from Bacillus subtilis K‐1
    Satbir Singh, Puneet Gupta, Bijender K. Bajaj
    Journal of Basic Microbiology.2018; 58(1): 88.     CrossRef
  • Potential application spectrum of microbial proteases for clean and green industrial production
    Satbir Singh, Bijender Kumar Bajaj
    Energy, Ecology and Environment.2017; 2(6): 370.     CrossRef
  • Improvement of enzyme activity and soluble expression of an alkaline protease isolated from oil-polluted mud flat metagenome by random mutagenesis
    Bo-Liang Gong, Run-Qian Mao, Yue Xiao, Mei-Lu Jia, Xiao-Lin Zhong, Yan Liu, Pei-Lin Xu, Gang Li
    Enzyme and Microbial Technology.2017; 106: 97.     CrossRef
  • Purification and Characterization of Halophilic Organic Solvent Tolerant Protease from Marine Bacillus sp. APCMST-RS7 and Its Antioxidant Potentials
    Thirumalai Maruthiah, Grasian Immanuel, Arunachalam Palavesam
    Proceedings of the National Academy of Sciences, India Section B: Biological Sciences.2017; 87(1): 207.     CrossRef
  • Production, purification and characterization of a thermotolerant alkaline serine protease from a novel species Bacillus caseinilyticus
    Thirumala Mothe, Vishnuvardhan Reddy Sultanpuram
    3 Biotech.2016;[Epub]     CrossRef
  • Effects of soybean meal replacement with fermented alfalfa meal on the growth performance, serum antioxidant functions, digestive enzyme activities, and cecal microflora of geese
    Hai-cheng YIN, Jin HUANG
    Journal of Integrative Agriculture.2016; 15(9): 2077.     CrossRef
  • Purification and Characterization of a Halotolerant Alkaline Serine Protease fromPenicillium citrinumYL-1 Isolated from Traditional Chinese Fish Sauce
    Li Xie, Yunzhu Xiao, Xiangyang Gao
    Food Biotechnology.2016; 30(2): 137.     CrossRef
  • Purification and Characterization of a Thermo- and Organic Solvent-Tolerant Alkaline Protease fromBacillussp. JER02
    Arastoo Badoei-Dalfard, Zahra Karami, Hadi Ravan
    Preparative Biochemistry and Biotechnology.2015; 45(2): 128.     CrossRef
  • Purification, biochemical characterization and structural modeling of a potential htrA-like serine protease from Bacillus subtilis DR8806
    Shaghayegh Farhadian, Ahmad Asoodeh, Milad Lagzian
    Journal of Molecular Catalysis B: Enzymatic.2015; 115: 51.     CrossRef
  • Isolation, Purification and Characterisation of an Organic Solvent-Tolerant Ca2+-Dependent Protease from Bacillus megaterium AU02
    J Deepa Arul Priya, K Divakar, M Suryia Prabha, G Panneer Selvam, Pennathur Gautam
    Applied Biochemistry and Biotechnology.2014; 172(2): 910.     CrossRef
  • Biochemical and structural characterization of a detergent-stable serine alkaline protease from seawater haloalkaliphilic bacteria
    Vikram H. Raval, Sumitha Pillai, Chirantan M. Rawal, Satya P. Singh
    Process Biochemistry.2014; 49(6): 955.     CrossRef
  • Multifarious potential applications of keratinase ofBacillus subtilisK-5
    Satbir Singh, Puneet Gupta, Vishal Sharma, Shweta Koul, Kamaldeep Kour, Bijender Kumar Bajaj
    Biocatalysis and Biotransformation.2014; 32(5-6): 333.     CrossRef
  • Effects of dietary inclusion of fermented cottonseed meal on growth, cecal microbial population, small intestinal morphology, and digestive enzyme activity of broilers
    Hong Sun, Jiang-wu Tang, Xiao-hong Yao, Yi-fei Wu, Xin Wang, Jie Feng
    Tropical Animal Health and Production.2013; 45(4): 987.     CrossRef
  • Fermentation and Quality Characteristics of Cheonggukjang Fermented with Bacillus subtilis BC-P1
    Sung-Yong Park, Mi-Ae Bang, Boung-Jun Oh, Jeong-Hoon Park, Won-Seob Song, Kyung-Min Choi, Eui-Su Choung, Hee-Ock Boo, Seung-Sik Cho
    The Korean Journal of Microbiology.2013; 49(3): 262.     CrossRef
  • IMMOBILIZATION OF CARBONIC ANHYDRASE ENZYME PURIFIED FROMBacillus subtilisVSG-4 AND ITS APPLICATION AS CO2SEQUESTERER
    M. Oviya, Sib Sankar Giri, V. Sukumaran, P. Natarajan
    Preparative Biochemistry and Biotechnology.2012; 42(5): 462.     CrossRef
Journal Article
Cloning, Expression, and Characterization of Serine Protease from Thermophilic Fungus Thermoascus aurantiacus var. levisporus
An-Na Li , Chen Xie , Jie Zhang , Jia Zhang , Duo-Chuan Li
J. Microbiol. 2011;49(1):121-129.   Published online March 3, 2011
DOI: https://doi.org/10.1007/s12275-011-9355-6
  • 290 View
  • 0 Download
  • 9 Crossref
AbstractAbstract PDF
The serine protease gene from a thermophilic fungus Thermoascus aurantiacus var. levisporus, was cloned, sequenced, and expressed in Pichia pastoris and the recombinant protein was characterized. The full-length cDNA of 2,592 bp contains an ORF of 1,482 bp encoding 494 amino acids. Sequence analysis of the deduced amino acid sequence revealed high homology with subtilisin serine proteases. The putative enzyme contained catalytic domain with active sites formed by three residues of Asp183, His215, and Ser384. The molecular mass of the recombinant enzyme was estimated to be 59.1 kDa after overexpression in P. pastoris. The activity of recombinant protein was 115.58 U/mg. The protease exhibited its maximal activity at 50°C and pH 8.0 and kept thermostable at 60°C, and retained 60% activity after 60 min at 70°C. The protease activity was found to be inhibited by PMSF, but not by DTT or EDTA. The enzyme has broad substrate specificity such as gelatin, casein and pure milk, and exhibiting highest activity towards casein.

Citations

Citations to this article as recorded by  
  • A Novel C-Terminal Small Tail Provides Thermostability of FeSOD Implying a New Mechanism of Protein Heat Resistance
    Weina Lu, Zhuo Jiang, Qi Lin, Zhecheng Yang, Yanli Liu, Wenhui Bi, Zhengying You, Caiying Jiang, Qing Sheng, Zuoming Nie
    The Protein Journal.2025; 44(5): 570.     CrossRef
  • Microbial proteases and their applications
    Peng Song, Xue Zhang, Shuhua Wang, Wei Xu, Fei Wang, Rongzhao Fu, Feng Wei
    Frontiers in Microbiology.2023;[Epub]     CrossRef
  • Improving the catalytic activity of a detergent‐compatible serine protease by rational design
    Xiao Wang, Xing Qin, Lige Tong, Jie Zheng, Tao Dong, Xiaolu Wang, Yuan Wang, Huoqing Huang, Bin Yao, Honglian Zhang, Huiying Luo
    Microbial Biotechnology.2023; 16(5): 947.     CrossRef
  • Identification of Exoenzymes Secreted by Entomopathogenic Fungus Beauveria pseudobassiana RGM 2184 and Their Effect on the Degradation of Cocoons and Pupae of Quarantine Pest Lobesia botrana
    Matias Arias-Aravena, Fabiola Altimira, Daniela Gutiérrez, Jian Ling, Eduardo Tapia
    Journal of Fungi.2022; 8(10): 1083.     CrossRef
  • Heterologous expression and characterization of a novel subtilisin-like protease from a thermophilic Thermus thermophilus HB8
    Guiqiu Xie, Zhengkang Shao, Li Zong, Xingxing Li, Dengli Cong, Rui Huo
    International Journal of Biological Macromolecules.2019; 138: 528.     CrossRef
  • Purification and characterization of cloned alkaline protease gene of Geobacillus stearothermophilus
    Irfana Iqbal, Muhammad Nauman Aftab, Mohammed Afzal, Asad Ur‐Rehman, Saima Aftab, Asma Zafar, Zia Ud‐Din, Ateeque Rahman Khuharo, Jawad Iqbal, Ikram Ul‐Haq
    Journal of Basic Microbiology.2015; 55(2): 160.     CrossRef
  • Enhancing xylanase production in the thermophilic fungus Myceliophthora thermophila by homologous overexpression of Mtxyr1
    Juan Wang, Yaning Wu, Yanfen Gong, Shaowen Yu, Gang Liu
    Journal of Industrial Microbiology and Biotechnology.2015; 42(9): 1233.     CrossRef
  • MS Analysis and Molecular Characterization of Botrytis cinerea Protease Prot-2. Use in Bioactive Peptides Production
    Ferid Abidi, Nayssene Aissaoui, Jean-Charles Gaudin, Jean-Marc Chobert, Thomas Haertlé, Mohamed Nejib Marzouki
    Applied Biochemistry and Biotechnology.2013; 170(2): 231.     CrossRef
  • Characterization, cloning, and heterologous expression of a subtilisin-like serine protease gene VlPr1 from Verticillium lecanii
    Gang Yu, Jin-Liang Liu, Li-Qin Xie, Xue-Liang Wang, Shi-Hong Zhang, Hong-Yu Pan
    Journal of Microbiology.2012; 50(6): 939.     CrossRef
Research Support, Non-U.S. Gov'ts
Diversity of Cold-Active Protease-Producing Bacteria from Arctic Terrestrial and Marine Environments Revealed by Enrichment Culture
Eun Hye Kim , Kyeung Hee Cho , Yung Mi Lee , Joung Han Yim , Hong Kum Lee , Jang-Cheon Cho , Soon Gyu Hong
J. Microbiol. 2010;48(4):426-432.   Published online August 20, 2010
DOI: https://doi.org/10.1007/s12275-010-0015-z
  • 350 View
  • 0 Download
  • 22 Crossref
AbstractAbstract PDF
A new approach for enrichment culture was applied to obtain cold-active protease-producing bacteria for marine and terrestrial samples from Svalbard, Norway. The method was developed for the enrichment of bacteria by long-term incubation at low temperatures in semi-solid agar medium containing meat pieces as the main source of carbon and energy. ZoBell and 0.1× nutrient broth were added for marine and terrestrial microorganisms, respectively, to supply basal elements for growth. One to three types of colonies were observed from each enrichment culture, indicating that specific bacterial species were enriched during the experimental conditions. Among 89 bacterial isolates, protease activity was observed from 48 isolates in the screening media containing skim milk. Good growth was observed at 4°C and 10°C while none of the isolates could grow at 37°C. At low temperatures, enzyme activity was equal to or higher than activity at higher temperatures. Bacterial isolates were included in the genera Pseudoalteromonas (33 isolates), Arthrobacter (24 isolates), Pseudomonas (16 isolates), Psychrobacter (6 isolates), Sphingobacterium (6 isolates), Flavobacterium (2 isolates), Sporosarcina (1 isolate), and Stenotrophomonas (1 isolate). Protease activity was observed from Pseudoalteromonas (33 isolates), Pseudomonas (10 isolates), Arthrobacter (4 isolates), and Flavobacterium (1 isolate).

Citations

Citations to this article as recorded by  
  • Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst
    Zhengfeng Yang, Zhendi Huang, Qian Wu, Xianghua Tang, Zunxi Huang
    International Journal of Molecular Sciences.2023; 24(10): 8532.     CrossRef
  • Five decades of terrestrial and freshwater research at Ny-Ålesund, Svalbard
    Å.Ø. Pedersen, P. Convey, K.K. Newsham, J.B. Mosbacher, E. Fuglei, V. Ravolainen, B.B. Hansen, T.C. Jensen, A. Augusti, E.M. Biersma, E.J. Cooper, S.J. Coulson, G.W. Gabrielsen, J.C. Gallet, U. Karsten, S.M. Kristiansen, M.M. Svenning, A.T. Tveit, M. Uchi
    Polar Research.2022;[Epub]     CrossRef
  • An Updated review on production of food derived bioactive peptides; focus on the psychrotrophic bacterial proteases
    Hossein Ahangari, Parivar Yazdani, Vida Ebrahimi, Saiedeh Razi Soofiyani, Robab Azargun, Vahideh Tarhriz, Shirin Eyvazi
    Biocatalysis and Agricultural Biotechnology.2021; 35: 102051.     CrossRef
  • Proteases from the marine bacteria in the genus Pseudoalteromonas: diversity, characteristics, ecological roles, and application potentials
    Xiu-Lan Chen, Yan Wang, Peng Wang, Yu-Zhong Zhang
    Marine Life Science & Technology.2020; 2(4): 309.     CrossRef
  • DISCOVERY OF COLD-ACTIVE PROTEASE FROM PSYCHROPHILIC BACTERIA ISOLATED FROM ANTARCTIC REGION FOR BIO-PROSPECTING
    MUHAMMAD ASYRAF ABD LATIP, SITI AISYAH ALIAS, SMYKLA JERZY, FARIDAH YUSOF, MOHD AZRUL NAIM MOHAMAD, NOOR FAIZUL HADRY NORDIN
    Malaysian Applied Biology.2020; 49(1): 55.     CrossRef
  • Genomic and Metabolomic Analysis of Antarctic Bacteria Revealed Culture and Elicitation Conditions for the Production of Antimicrobial Compounds
    Kattia Núñez-Montero, Damián Quezada-Solís, Zeinab Khalil, Robert Capon, Fernando Andreote, Leticia Barrientos
    Biomolecules.2020; 10(5): 673.     CrossRef
  • Quantification of Extracellular Proteases and Chitinases from Marine Bacteria
    Yang Zou, Johan Robbens, Marc Heyndrickx, Jane Debode, Katleen Raes
    Current Microbiology.2020; 77(12): 3927.     CrossRef
  • Adaptation, production, and biotechnological potential of cold-adapted proteases from psychrophiles and psychrotrophs: recent overview
    Junaid Furhan
    Journal of Genetic Engineering and Biotechnology.2020; 18(1): 36.     CrossRef
  • Culture-Dependent and -Independent Analyses Reveal the Diversity, Structure, and Assembly Mechanism of Benthic Bacterial Community in the Ross Sea, Antarctica
    An-Zhang Li, Xi-Bin Han, Ming-Xia Zhang, Yang Zhou, Meng Chen, Qing Yao, Hong-Hui Zhu
    Frontiers in Microbiology.2019;[Epub]     CrossRef
  • Analysis of the bacterial community from high alkaline (pH > 13) drainage water at a brown mud disposal site near Žiar nad Hronom (Banská Bystrica region, Slovakia) using 454 pyrosequencing
    Jana Kisková, Zuzana Stramová, Peter Javorský, Jana Sedláková-Kaduková, Peter Pristaš
    Folia Microbiologica.2019; 64(1): 83.     CrossRef
  • Cold active pectinase, amylase and protease production by yeast isolates obtained from environmental samples
    Ceren Daskaya-Dikmen, Funda Karbancioglu-Guler, Beraat Ozcelik
    Extremophiles.2018; 22(4): 599.     CrossRef
  • Sphingobactan, a new α-mannan exopolysaccharide from Arctic Sphingobacterium sp. IITKGP-BTPF3 capable of biological response modification
    Soumya Chatterjee, Sourav K. Mukhopadhyay, Samiran S. Gauri, Satyahari Dey
    International Immunopharmacology.2018; 60: 84.     CrossRef
  • Advances in Antarctic Research for Antimicrobial Discovery: A Comprehensive Narrative Review of Bacteria from Antarctic Environments as Potential Sources of Novel Antibiotic Compounds Against Human Pathogens and Microorganisms of Industrial Importance
    Kattia Núñez-Montero, Leticia Barrientos
    Antibiotics.2018; 7(4): 90.     CrossRef
  • The pangenome of (Antarctic) Pseudoalteromonas bacteria: evolutionary and functional insights
    Emanuele Bosi, Marco Fondi, Valerio Orlandini, Elena Perrin, Isabel Maida, Donatella de Pascale, Maria Luisa Tutino, Ermenegilda Parrilli, Angelina Lo Giudice, Alain Filloux, Renato Fani
    BMC Genomics.2017;[Epub]     CrossRef
  • Enhanced production of protease by Pseudoalteromonas arctica PAMC 21717 via statistical optimization of mineral components and fed-batch fermentation
    Se Jong Han, Heeyong Park, Sunghui Kim, Dockyu Kim, Ha Ju Park, Joung Han Yim
    Preparative Biochemistry & Biotechnology.2016; 46(4): 328.     CrossRef
  • Anthranilate degradation by a cold‐adapted Pseudomonas sp. 
    Dockyu Kim, Miyoun Yoo, Eungbin Kim, Soon Gyu Hong
    Journal of Basic Microbiology.2015; 55(3): 354.     CrossRef
  • A comparison of pelagic, littoral, and riverine bacterial assemblages in Lake Bangongco, Tibetan Plateau
    Yongqin Liu, John C. Priscu, Tandong Yao, Trista J. Vick-Majors, Alexander B. Michaud, Nianzhi Jiao, Juzhi Hou, Lide Tian, Anyi Hu, Zhong-Qiang Chen
    FEMS Microbiology Ecology.2014; 89(2): 211.     CrossRef
  • Bioactive peptides from caseins released by cold active proteolytic enzymes from Arsukibacterium ikkense
    Cristian De Gobba, Gorazd Tompa, Jeanette Otte
    Food Chemistry.2014; 165: 205.     CrossRef
  • Isolation and physiological characterization of psychrophilic denitrifying bacteria from permanently cold Arctic fjord sediments (Svalbard, Norway)
    Andy Canion, Om Prakash, Stefan J. Green, Linda Jahnke, Marcel M. M. Kuypers, Joel E. Kostka
    Environmental Microbiology.2013; 15(5): 1606.     CrossRef
  • Enzymes from the gut bacteria of Atlantic cod, Gadus morhua and their influence on intestinal enzyme activity
    C.C. LAZADO, C.M.A. CAIPANG, V. KIRON
    Aquaculture Nutrition.2012; 18(4): 423.     CrossRef
  • Polar and Alpine Microbial Collection (PAMC): a culture collection dedicated to polar and alpine microorganisms
    Yung Mi Lee, GoHeung Kim, You-Jung Jung, Cheng-Dae Choe, Joung Han Yim, Hong Kum Lee, Soon Gyu Hong
    Polar Biology.2012; 35(9): 1433.     CrossRef
  • Analysis and comparison of the microflora isolated from fresco surface and from surrounding air environment through molecular and biodegradative assays
    Domenico Pangallo, Lucia Kraková, Katarína Chovanová, Alexandra Šimonovičová, Filomena De Leo, Clara Urzì
    World Journal of Microbiology and Biotechnology.2012; 28(5): 2015.     CrossRef
Production, Partial Characterization, and Immobilization in Alginate Beads of an Alkaline Protease from a New Thermophilic Fungus Myceliophthora sp.
Letícia Maria Zanphorlin , Fernanda Dell Antonio Facchini , Filipe Vasconcelos , Rafaella Costa Bonugli-Santos , André Rodrigues , Lara Durães Sette , Eleni Gomes , Gustavo Orlando Bonilla-Rodriguez
J. Microbiol. 2010;48(3):331-336.   Published online June 23, 2010
DOI: https://doi.org/10.1007/s12275-010-9269-8
  • 275 View
  • 0 Download
  • 25 Crossref
AbstractAbstract PDF
Thermophilic fungi produce thermostable enzymes which have a number of applications, mainly in biotechnological processes. In this work, we describe the characterization of a protease produced in solidstate (SSF) and submerged (SmF) fermentations by a newly isolated thermophilic fungus identified as a putative new species in the genus Myceliophthora. Enzyme-production rate was evaluated for both fermentation processes, and in SSF, using a medium composed of a mixture of wheat bran and casein, the proteolytic output was 4.5-fold larger than that obtained in SmF. Additionally, the peak of proteolytic activity was obtained after 3 days for SSF whereas for SmF it was after 4 days. The crude enzyme obtained by both SSF and SmF displayed similar optimum temperature at 50°C, but the optimum pH shifted from 7 (SmF) to 9 (SSF). The alkaline protease produced through solid-state fermentation (SSF), was immobilized on beads of calcium alginate, allowing comparative analyses of free and immobilized proteases to be carried out. It was observed that both optimum temperature and thermal stability of the immobilized enzyme were higher than for the free enzyme. Moreover, the immobilized enzyme showed considerable stability for up to 7 reuses.

Citations

Citations to this article as recorded by  
  • Production and Potential Application of an Alkaline Serine Peptidase from Myceliophtora heterothallica for Biofilm Removal
    Rafael Amadeu Barreto, Emanuella Roberto Ribeiro, Cíntia Lionela Ambrósio de Menezes, Mohammed Anas Zaiter, Maurício Boscolo, Roberto da Silva, Eleni Gomes, Ronivaldo Rodrigues da Silva
    Current Microbiology.2025;[Epub]     CrossRef
  • Heterologous expression of GH11 xylanase from Myceliophthora heterothallica F.2.1.4 in Pichia pastoris
    Gabriela Salvador de Amo, Carolina Bezerra-Bussoli, Ronivaldo Rodrigues da Silva, Luciano Takeshi Kishi, Henrique Ferreira, Eleni Gomes, Gustavo Orlando Bonilla-Rodriguez
    Biocatalysis and Agricultural Biotechnology.2024; 61: 103343.     CrossRef
  • Production, optimization, and purification of alkaline thermotolerant protease from newly isolated Phalaris minor seeds
    Umber Zaman, Khalil ur Rehman, Shahid Ullah Khan, Syed Badshah, Khaled M. Hosny, Majd A. Alghamdi, Hatem K. Hmid, Mohammed Alissa, Deena M. Bukhary, Ehab A. Abdelrahman
    International Journal of Biological Macromolecules.2023; 233: 123544.     CrossRef
  • Purification and Characterization of Alkaline Protease Isolated from Cotton (Gossypium hirsutum) Seeds
    Asghar Ali Shaikh, Muhammad Umer Dahot, Abdul Sajid, Syed Habib Ahmed Naqvi
    Journal of Applied Research in Plant Sciences .2023; 5(01): 34.     CrossRef
  • Biocatalytic Profiling of Free and Immobilized Partially Purified Alkaline Protease from an Autochthonous Bacillus aryabhattai Ab15-ES
    Adegoke Isiaka Adetunji, Ademola Olufolahan Olaniran
    Reactions.2023; 4(2): 231.     CrossRef
  • Fungal alkaline proteases and their potential applications in different industries
    Kadambari Subhash Pawar, Paras Nath Singh, Sanjay Kumar Singh
    Frontiers in Microbiology.2023;[Epub]     CrossRef
  • Valorization of agricultural residues using Myceliophthora thermophila as a platform for production of lignocellulolytic enzymes for cellulose saccharification
    Nathália Gonsales da Rosa-Garzon, Hélen Julie Laure, José César Rosa, Hamilton Cabral
    Biomass and Bioenergy.2022; 161: 106452.     CrossRef
  • Immobilized fungal enzymes: Innovations and potential applications in biodegradation and biosynthesis
    Yifan Gao, Kshitjia Shah, Ivy Kwok, Meng Wang, Leonard H. Rome, Shaily Mahendra
    Biotechnology Advances.2022; 57: 107936.     CrossRef
  • An Overview of Proteases: Production, Downstream Processes and Industrial Applications
    Nathiele Contrera Gimenes, Edgar Silveira, Elias Basile Tambourgi
    Separation & Purification Reviews.2021; 50(3): 223.     CrossRef
  • Optimization of protease production from Bacillus halodurans under solid state fermentation using agrowastes
    Chellapandian Balachandran, Alagumalai Vishali, Natarajan Arun Nagendran, Kathirvelu Baskar, Abeer Hashem, Elsayed Fathi Abd_Allah
    Saudi Journal of Biological Sciences.2021; 28(8): 4263.     CrossRef
  • Bioassay guided fractionation of bioactive metabolite from Corynascus verrucosus inhabiting Croton bonplandianus Baill
    N. Chandra Mohana, D. Rakshith, H.C. Yashavantha Rao, K.P. Ramesha, B.R. Nuthan, S. Satish
    Process Biochemistry.2020; 98: 106.     CrossRef
  • Characterization and immobilization of protease secreted by the fungus Moorella speciosa
    Juliana Mota de Oliveira, Pedro Fernandes, Raquel Guimarães Benevides, Sandra Aparecida de Assis
    3 Biotech.2020;[Epub]     CrossRef
  • Protease Production from Cheotomium globusum Through Central Composite Design Using Agricultural Wastes and Its Immobilization for Industrial Exploitation
    Fareeha Nadeem, Tahir Mehmood, Muhammad Naveed, Shazia Shamas, Tasmia Saman, Zahid Anwar
    Waste and Biomass Valorization.2020; 11(12): 6529.     CrossRef
  • Heterologous expression, purification and biochemical characterization of a new xylanase from Myceliophthora heterothallica F.2.1.4
    Gabriela Salvador de Amo, Carolina Bezerra-Bussoli, Ronivaldo Rodrigues da Silva, Luciano Takeshi Kishi, Henrique Ferreira, Ricardo Barros Mariutti, Raghuvir Krishnaswamy Arni, Eleni Gomes, Gustavo Orlando Bonilla-Rodriguez
    International Journal of Biological Macromolecules.2019; 131: 798.     CrossRef
  • Purification and Physicochemical Characterization of a Novel Thermostable Xylanase Secreted by the Fungus Myceliophthora heterothallica F.2.1.4
    Lorena Caixeta de Oliveira Simões, Ronivaldo Rodrigues da Silva, Carlos Eduardo de Oliveira Nascimento, Maurício Boscolo, Eleni Gomes, Roberto da Silva
    Applied Biochemistry and Biotechnology.2019; 188(4): 991.     CrossRef
  • Study on immobilization of papain with magnetic porous alginate microspheres
    Hui Wang, Dongxu Shao
    IOP Conference Series: Materials Science and Engineering.2018; 397: 012031.     CrossRef
  • Partitioning and extraction protease from Aspergillus tamarii URM4634 using PEG-citrate aqueous two-phase systems
    Osmar Soares da Silva, Matheus Henrique Gouveia Gomes, Rodrigo Lira de Oliveira, Ana Lúcia Figueiredo Porto, Attilio Converti, Tatiana Souza Porto
    Biocatalysis and Agricultural Biotechnology.2017; 9: 168.     CrossRef
  • Biochemical properties of a serine protease fromAspergillus flavusand application in dehairing
    Daniel Guerra Franco, Regiane Nogueira Spalanzani, Emmly Ernesto Lima, Clarice Rossato Marchetti, Patrícia Oliveira Silva, Douglas Chodi Masui, Giovana Cristina Giannesi, Fabiana Fonseca Zanoelo
    Biocatalysis and Biotransformation.2017; 35(4): 249.     CrossRef
  • Bioprocess optimization for production of thermoalkali-stable protease from Bacillus subtilis K-1 under solid-state fermentation
    Satbir Singh, Bijender Kumar Bajaj
    Preparative Biochemistry & Biotechnology.2016; 46(7): 717.     CrossRef
  • Purification and characterization of an extracellular haloalkaline serine protease from the moderately halophilic bacterium, Bacillus iranensis (X5B)
    Hossein Ghafoori, Mansoure Askari, Sajjad Sarikhan
    Extremophiles.2016; 20(2): 115.     CrossRef
  • Novel Protease from <i>Aspergillus tamarii</i> URM4634: Production and Characterization Using Inexpensive Agroindustrial Substrates by Solid-State Fermentation
    Osmar Soares da Silva, Rodrigo Lira de Oliveira, Cristina Maria Souza-Motta, Ana Lúcia Figueiredo Porto, Tatiana Souza Porto
    Advances in Enzyme Research.2016; 04(04): 125.     CrossRef
  • Production, optimization and partial purification of protease fromBacillus subtilis
    Gaurav Pant, Anil Prakash, J.V.P. Pavani, Sayantan Bera, G.V.N.S. Deviram, Ajay Kumar, Mitali Panchpuri, Ravi Gyana Prasuna
    Journal of Taibah University for Science.2015; 9(1): 50.     CrossRef
  • Production and Characterization of New Fibrinolytic Protease from <i>Mucor subtillissimus</i> UCP 1262 in Solid-State Fermentation
    Thiago Pajeú Nascimento, Amanda Emmanuelle Sales, Camila Souza Porto, Romero Marcos Pedrosa Brandão, Galba Maria Campos Takaki, Jose Antônio Couto Teixeira, Tatiana Souza Porto, Ana Lúcia Figueiredo Porto
    Advances in Enzyme Research.2015; 03(03): 81.     CrossRef
  • Immobilization of halophilic Bacillus sp. EMB9 protease on functionalized silica nanoparticles and application in whey protein hydrolysis
    Rajeshwari Sinha, S. K. Khare
    Bioprocess and Biosystems Engineering.2015; 38(4): 739.     CrossRef
  • Purification and characterization of a new alkaline serine protease from the thermophilic fungus Myceliophthora sp.
    L.M. Zanphorlin, H. Cabral, E. Arantes, D. Assis, L. Juliano, M.A. Juliano, R. Da-Silva, E. Gomes, G.O. Bonilla-Rodriguez
    Process Biochemistry.2011; 46(11): 2137.     CrossRef
Taxonomic Revision of the Nematode-Trapping Fungus Arthrobotrys multisecundaria
Juan Li , Jinkui Yang , Lianming Liang , Ke-Qin Zhang
J. Microbiol. 2008;46(5):513-518.   Published online October 31, 2008
DOI: https://doi.org/10.1007/s12275-007-0115-6
  • 257 View
  • 0 Download
  • 5 Crossref
AbstractAbstract PDF
The gene encoding an extracellular serine protease was cloned from Arthrobotrys multisecundaria using degenerate primers. The gene was highly similar (99.26%) to protease Mlx from Monacrosporium microscaphoides. To clarify the taxonomic relationship between these species, genes encoding the internal transcribed spacer (ITS) and β-tubulin were also cloned and sequenced from A. multisecundaria and M. microscaphoides, respectively. Homologous analysis of the nuclear (ITS) and protein (β-tubulin) encoding genes showed that the two species of nematode-trapping fungi also shared extensive identity (99.82 and 99.63%, respectively), although they exhibited obvious differences in secondary conidia morphology. Accordingly, a taxonomic revision is recommended, with A. multisecundaria being revised as A. microscaphoides var. multisecundaria. In addition, the identified mutation may better facilitate the study of the sporulation of nematode-trapping fungi.

Citations

Citations to this article as recorded by  
  • Unveiling community patterns and trophic niches of tropical and temperate ants using an integrative framework of field data, stable isotopes and fatty acids
    Felix B. Rosumek, Nico Blüthgen, Adrian Brückner, Florian Menzel, Gerhard Gebauer, Michael Heethoff
    PeerJ.2018; 6: e5467.     CrossRef
  • Relationship between environmental conditions,TRI5 gene expression and deoxynivalenol production in storedLentinula edodes infected withFusarium graminearum
    Z. Han, Y. Shen, J. Diana Di Mavungu, D. Zhang, D. Nie, K. Jiang, S. De Saeger, Z. Zhao
    World Mycotoxin Journal.2018; 11(2): 177.     CrossRef
  • Notes for genera: Ascomycota
    Nalin N. Wijayawardene, Kevin D. Hyde, Kunhiraman C. Rajeshkumar, David L. Hawksworth, Hugo Madrid, Paul M. Kirk, Uwe Braun, Rajshree V. Singh, Pedro W. Crous, Martin Kukwa, Robert Lücking, Cletus P. Kurtzman, Andrey Yurkov, Danny Haelewaters, André Aptro
    Fungal Diversity.2017; 86(1): 1.     CrossRef
  • Genetic diversity of microorganisms
    Juan LI, Ke-Qin ZHANG
    Hereditas (Beijing).2012; 34(11): 1399.     CrossRef
  • BIHARMONIC LEGENDRE CURVES IN SASAKIAN SPACE FORMS
    Dorel Fetcu
    Journal of the Korean Mathematical Society.2008; 45(2): 393.     CrossRef
Two Forms of Vibrio vulnificus Metalloprotease VvpE are Secreted via the Type II General Secretion System
Jong Park , So-Yeon Ryu , Choon-Mee Kim , Sung-Heui Shin
J. Microbiol. 2008;46(3):338-343.   Published online July 5, 2008
DOI: https://doi.org/10.1007/s12275-008-0058-6
  • 283 View
  • 0 Download
  • 10 Crossref
AbstractAbstract PDF
Vibrio vulnificus has been known to secrete one form of metalloprotease VvpE (45 kDa) that is cleaved to 34 kDa-VvpE and 11 kDa-C-terminal propeptide via extracellular autoproteolysis. However, we found that extracellular secretion of both the 34 and 45 kDa forms of VvpE began in the early growth phase; moreover, 34 kDa-VvpE existed as the major form in V. vulnificus cell lysates and culture supernatants. In addition, extracellular secretion of both 34 and 45 kDa-VvpE was blocked by mutation of the pilD gene, which encodes for the type IV leader peptidase/N-methyltransferase of the type II general secretion system, and the blocked VvpE secretion was recovered by in trans-complementation of the wild-type pilD gene. These results indicate that 34 kDa-VvpE is the major form secreted along with 45 kDa-VvpE from the early growth phase via the PilD-mediated type II general secretion system.

Citations

Citations to this article as recorded by  
  • Structure and assembly of pilotin-dependent and -independent secretins of the type II secretion system
    S. Peter Howard, Leandro F. Estrozi, Quentin Bertrand, Carlos Contreras-Martel, Timothy Strozen, Viviana Job, Alexandre Martins, Daphna Fenel, Guy Schoehn, Andréa Dessen, Tomoko Kubori
    PLOS Pathogens.2019; 15(5): e1007731.     CrossRef
  • Bacterial calpains and the evolution of the calpain (C2) family of peptidases
    Neil D. Rawlings
    Biology Direct.2015;[Epub]     CrossRef
  • Vibrio vulnificus quorum-sensing system operates in cirrhotic ascites, a human ex vivo experimental system
    Choon-Mee Kim, Sung-Heui Shin
    Annals of Microbiology.2013; 63(1): 403.     CrossRef
  • SmcR, the Quorum-sensing Master Regulator, Is Partially Involved in Temperature/Salinity-mediated Changes in MetalloproteasevvpEExpression inVibrio vulnificus
    Choon-Mee Kim, Sung-Heui Shin
    Journal of Bacteriology and Virology.2012; 42(1): 29.     CrossRef
  • Change ofVibrio vulnificusMetalloprotease VvpE Production by Temperature and Salinity
    Choon-Mee Kim, Sung-Heui Shin
    Journal of Bacteriology and Virology.2011; 41(3): 147.     CrossRef
  • Functional Characterization of EpsC, a Component of the Type II Secretion System, in the Pathogenicity of Vibrio vulnificus
    Won Hwang, Na Yeon Lee, Juri Kim, Mi-Ae Lee, Kun-Soo Kim, Kyu-Ho Lee, Soon-Jung Park, S. R. Blanke
    Infection and Immunity.2011; 79(10): 4068.     CrossRef
  • Genomic and proteomic analyses of the coral pathogen Vibrio coralliilyticus reveal a diverse virulence repertoire
    Eidy de O Santos, Nelson Alves, Graciela M Dias, Ana Maria Mazotto, Alane Vermelho, Gary J Vora, Bryan Wilson, Victor H Beltran, David G Bourne, Frédérique Le Roux, Fabiano L Thompson
    The ISME Journal.2011; 5(9): 1471.     CrossRef
  • Proteases Produced by Vibrios
    SUMIO SHINODA, SHIN-ICHI MIYOSHI
    Biocontrol Science.2011; 16(1): 1.     CrossRef
  • A recombinant metalloprotease antigen ofVibrio vulnificuselicits protective antibodies in a murine model
    Y.-C. Chen, C.-C. Chang, S.-Y. Chang, J.-H. Su
    Letters in Applied Microbiology.2010; 50(2): 168.     CrossRef
  • Current status and future prospects in a pathogenic study of Vibrio vulnificus
    Takashige KASHIMOTO
    Nippon Saikingaku Zasshi.2010; 65(3): 369.     CrossRef
InhA-Like Protease Secreted by Bacillus sp. S17110 Inhabited in Turban Shell
Sang Chul Jung , Hyoung-Rok Paik , Mi Sun Kim , Keun Sik Baik , Woo-Yiel Lee , Chi Nam Seong , Sang Ki Choi
J. Microbiol. 2007;45(5):402-408.
DOI: https://doi.org/2597 [pii]
  • 185 View
  • 0 Download
AbstractAbstract PDF
A strain producing a potent protease was isolated from turban shell. The strain was identified as Bacillus sp. S17110 based on phylogenetic analysis. The enzyme was purified from culture supernatant of Bacillus sp. S17110 to homogeneity by ammonium sulfate precipitation, SP-Sepharose, and DEAE-Sepharose anion exchange chromatography. Protease activity of the purified protein against casein was found to be stable at pH 7 to pH 10 and around 50°C. Approximately 70% of proteolytic activity of the enzyme was detected either in the presence of 100 mM SDS or Tween 20. The enzyme activity was enhanced in the presence of Ca2+, Zn2+, Mg2+, but was inhibited by EDTA, indicating that it requires metal for its activity. The purified enzyme was found to be a monomeric protein with a molecular mass of 75 kDa, as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography. The purified enzyme was analyzed through peptide fingerprint mass spectra generated from matrix-assisted laser desorption ionization-time-of-flight-mass spectrometry (MALDI-TOF-MS) and a BLAST search, and identified as immune inhibitor A (inhA) deduced from nucleotide sequence of B. cereus G9241. Since InhA was identified as protease that cleave antibacterial proteins found in insect, inhA-like protease purified from Bacillus sp. S17110 might be pathogenic to sea invertebrates.
Cloning and Expression of the Cathepsin F-like Cysteine Protease Gene in Escherichia coli and Its Characterization
Han Seung Joo , Kwang Bon Koo , Kyung In Park , Song Hwan Bae , Jong Won Yun , Chung Soon Chang , Jang Won Choi
J. Microbiol. 2007;45(2):158-167.
DOI: https://doi.org/2518 [pii]
  • 214 View
  • 0 Download
AbstractAbstract PDF
In this study, we have cloned a novel cDNA encoding for a papain-family cysteine protease from the Uni-ZAP XR cDNA library of the polychaete, Periserrula leucophryna. This gene was expressed in Escherichia coli using the T7 promoter system, and the protease was characterized after partial purification. First, the partial DNA fragment (498 bp) was amplified from the total RNA via RT-PCR using degenerated primers derived from the conserved region of cysteine protease. The full-length cDNA of cysteine protease (PLCP) was prepared via the screening of the Uni-ZAP XR cDNA library using the 32P-labeled partial DNA fragment. As a result, the PLCP gene was determined to consist of a 2591 bp nucleotide sequence (CDS: 173-1024 bp) which encodes for a 283-amino acid polypeptide, which is itself composed of an 59-residue signal sequence, a 6-residue propeptide, a 218-residue mature protein, and a long 3''-noncoding region encompassing 1564 bp. The predicted molecular weights of the preproprotein and the mature protein were calculated as 31.8 kDa and 25 kDa, respectively. The results of sequence analysis and alignment revealed a significant degree of sequence similarity with other eukaryotic cysteine proteases, including the conserved catalytic triad of the Cys90, His226, and Asn250 residues which characterize the C1 family of papain-like cysteine protease. The nucleotide and amino acid sequences of the novel gene were deposited into the GenBank database under the accession numbers, AY390282 and AAR27011, respectively. The results of Northern blot analysis revealed the 2.5 kb size of the transcript and ubiquitous expression throughout the entirety of the body, head, gut, and skin, which suggested that the PLCP may be grouped within the cathepsin F-like proteases. The region encoding for the mature form of the protease was then subcloned into the pT7-7 expression vector following PCR amplification using the designed primers, including the initiation and termination codons. The recombinant cysteine proteases were generated in a range of 6.3% to 12.5% of the total cell proteins in the E. coli BL21(DE3) strain for 8 transformants. The results of SDS-PAGE and Western blot analysis indicated that a cysteine protease of approximately 25 kDa (mature form) was generated. The optimal pH and temperature of the enzyme were determined to be approximately 9.5 and 35°C, respectively, thereby indicating that the cysteine protease is a member of the alkaline protease group. The evaluation of substrate specificity indicated that the purified protease was more active towards Arg-X or Lys-X and did not efficiently cleave the substrates with non-polar amino acids at the P1 site. The PLCP evidenced fibrinolytic activity on the plasminogen-free fibrin plate test.
A Fibrinolytic Enzyme from the Medicinal Mushroom Cordyceps militaris
Jae-Sung Kim , Kumar Sapkota , Se-Eun Park , Bong-Suk Choi , Seung Kim , Nguyen Thi Hiep , Chun-Sung Kim , Han-Seok Choi , Myung-Kon Kim , Hong-Sung Chun , Yeal Park , Sung-Jun Kim
J. Microbiol. 2006;44(6):622-631.
DOI: https://doi.org/2465 [pii]
  • 235 View
  • 0 Download
AbstractAbstract PDF
In this study we purified a fibrinolytic enzyme from Cordyceps militaris using a combination of ion-exchange chromatography on a DEAE Sephadex A-50 column, gel filtration chromatography on a Sephadex G-75 column, and FPLC on a HiLoad 16/60 Superdex 75 column. This purification protocol resulted in a 191.8-fold purification of the enzyme and a final yield of 12.9%. The molecular mass of the purified enzyme was estimated to be 52 kDa by SDS-PAGE, fibrin-zymography, and gel filtration chromatography. The first 19 amino acid residues of the N-terminal sequence were ALTTQSNV THGLATISLRQ, which is similar to the subtilisin-like serine protease PR1J from Metarhizium anisopliae var. anisopliase. This enzyme is a neutral protease with an optimal reaction pH and temperature of 7.4 and 37°C, respectively. Results for the fibrinolysis pattern showed that the enzyme rapidly hydrolyzed the fibrin α-chain followed by the γ-γ chains. It also hydrolyzed the β-chain, but more slowly. The Aα, Bβ, and γ chains of fibrinogen were also cleaved very rapidly. We found that enzyme activity was inhibited by Cu2+ and Co2+, but enhanced by the additions of Ca2+ and Mg2+ ions. Furthermore, fibrinolytic enzyme activity was potently inhibited by PMSF and APMSF. This enzyme exhibited a high specificity for the chymotrypsin substrate S-2586 indicating it’s a chymotrypsin-like serine protease. The data we present suggest that the fibrinolytic enzyme derived from the edible and medicinal mushroom Cordyceps militaris has fibrin binding activity, which allows for the local activation of the fibrin degradation pathway.
Vibrio vulnificus Metalloprotease VvpE has no Direct Effect on Iron-uptake from Human Hemoglobin
Hui-Yu Sun , Song-Iy Han , Mi-Hwa Choi , Seong-Jung Kim , Choon-Mee Kim , Sung-Heui Shin
J. Microbiol. 2006;44(5):537-547.
DOI: https://doi.org/2443 [pii]
  • 230 View
  • 0 Download
AbstractAbstract PDF
This study was designed to determine whether or not Vibrio vulnificus metalloprotease VvpE can promote iron uptake via the proteolytic cleavage of human hemoglobin. We found that V. vulnificus utilized hemoglobin as an iron source more efficiently via the vulnibactin-mediated iron-uptake system than via the HupA-mediated iron-uptake system and, of the proteases produced by V. vulnificus, VvpE was found to be the only protease capable of destroying hemoglobin. However, VvpE expression, on both the transcriptional and protein levels, was suppressed in iron-limited media. However, vvpE transcription, but not extracellular VvpE production, was reactivated by the addition of hemoglobin or inorganic iron into iron-limited media. Moreover, vvpE transcription began only in the late growth phase when V. vulnificus had already consumed most of the iron for growth. In addition, neither vvpE mutation nor in trans vvpE complementation affected the ability of V. vulnificus to acquire iron or to grow in iron-limited media or in cirrhotic ascites containing hemoglobin. Hemoglobin added into iron-limited media was not destroyed, but gradually formed an insoluble aggregate during culture; this aggregation of hemoglobin occurred regardless of vvpE mutation or complementation. These results indicate that VvpE is not required for efficient iron uptake from hemoglobin. On the contrary, hemoglobin or iron is required for efficient vvpE transcription. In addition, a discrepancy exists between vvpE transcription and extracellular VvpE production in iron-limited media containing inorganic iron or hemoglobin, which suggests that additional unknown posttranscriptional events may be involved in the extracellular production of VvpE.
Characterization of Calcium-Activated Bifunctional Peptidase of the Psychrotrophic Bacillus cereus
Jong-Il Kim , Sun-Min Lee , Hyun-Joo Jung
J. Microbiol. 2005;43(3):237-243.
DOI: https://doi.org/2219 [pii]
  • 226 View
  • 0 Download
AbstractAbstract PDF
The protease purified from Bacillus cereus JH108 has the function of leucine specific endopeptidase. When measured by hydrolysis of synthetic substrate (N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide), the enzyme activity exhibited optimal activity at pH 9.0, 60^oC. The endopeptidase activity was stimulated by Ca^+^+, Co^+^+, Mn^+^+, Mg^+^+, and Ni^+^+, and was inhibited by metal chelating agents such as EDTA, 1,10-phenanthroline, and EGTA. Addition of serine protease inhibitor, PMSF, resulted in the elimination of the activity. The endopeptidase activity was fully recovered from the inhibition of EDTA by the addition of 1 mM Ca^+^+, and was partially restored by Co^+^+ and Mn^+^+, indicating that the enzyme was stabilized and activated by divalent cations and has a serine residue at the active site. Addition of Ca^+^+ increased the pH and heat stability of endopeptidase activity. These results show that endopeptidase requires calcium ions for activity and/or stability. A Lineweaver-Burk plot analysis indicated that the K_m value of endopeptidase is 0.315 mM and V_max is 0.222 mmol of N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide per min. Bestatin was shown to act as a competitive inhibitor to the endopeptidase activity.
The Influence of NaCl and Carbonylcyanide-m-Chlorophenylhydrazone on the Production of Extracellular Proteases in a Marine Vibrio Strain
Young Jae Kim
J. Microbiol. 2004;42(2):156-159.
DOI: https://doi.org/2028 [pii]
  • 178 View
  • 0 Download
AbstractAbstract PDF
In general, the salinity of the ocean is close to 3.5% and marine vibrios possess the respiratory chainlinked Na+ pump. The influence of sodium chloride and the proton conductor carbonylcyanide m-chlorophenylhydrazone (CCCP) on the production of extracellular proteases in a marine Vibrio strain was examined. At the concentration of 0.5 M, sodium chloride minimally inhibited the activity of extracellular proteases by approximately 16%, whereas at the same concentration, the producton of extracellular proteases was severely inhibited. On the other hand, the production of extracellular proteases was completely inhibited by the addition of 2 μM CCCP at pH 8.5, where the respiratory chain-linked Na^+ pump functions.
Characteristics of protease inhibitor produced by streptomyces fradiae SMF9
Kim, Hyoung Tae , Suh, Joo Won , Lee, Key Joon
J. Microbiol. 1995;33(2):103-108.
  • 235 View
  • 0 Download
AbstractAbstract PDF
Streptomyces fradiae protease inhibitor (SFI) was purified effectively by preparative isoelectric focusing and hydroxyapatite chromatography. The molecular weight of SFI was estimated to be 1.7 kDa by SDS-PAGE and 1.8 kDa by molecular sieving HPLC. One hundred and sixty amino acid residues were determined from which molecular weight of SFI was calculated to be 17.054 Da and carbohydrate residue was not detected. SFI was calculated to be 17,064 Da and carbohydrate residue was not detected. SFI was a monomeric protein with two reactive sits, of which isoelectric point was pH 4.1. N-terminal amino acid sequence of SFI had homology with SSI (Streptomyces subsilisin inhibitor) and other protease inhibitors produced by Streptomyces.
Purification and Characterization of an Alkaline Protease produced by a Xanthomonas sp. YL-37
Lee, Chang Ho , Kim, Hee Sik , Kwon, Gi Soek , Oh, Hee Mock , Kang, Sang Mo , Kwon, Tae Jong , Yoon, Byung Dae
J. Microbiol. 1995;33(2):115-119.
  • 217 View
  • 0 Download
AbstractAbstract PDF
The alkaline protease of Xanthomonas sp. YL-37 has been purified, and the properties of the enzyme investigated. The alkaline protease of Xanthomonas sp. YL-37 was purified form crude enzyme by ammonium sulfate fractionation, CM-cellulose ion exchange chromatography, and Sephadex G-100 gel filtration. Through the series of chromatographies, the enzyme was purified to homogenecity with specific activity of 4.23 fold higher than that of the crude broth. The molecular weight of the purified protease has been estimated to be 62 KDa on SDS-polyacrylamide gel electrophoresis. The optimal pH and temperature for alkaline protease activity were 11.0 and 50℃, respectively. The enzyme was stable between pH 5.0 and 10.0 and up to 50℃. Enzyme activity was lost up to 50% on heating at 70℃ for 30 minutes. The activity of alkaline protease was inhibited by Cu^2+, Zn^2+, Hg^2+, PMSF, and activated by Mn^2+ and Ca^2+. The K_m value for casein as a substrate was 4.0 mg/ml.
Purification and Characterization of an Extracellular Protease from Culture Filtrate of Salmonella schttmulleri
Na, Byoung Kuk , Song, Chul Yong
J. Microbiol. 1995;33(3):244-251.
  • 255 View
  • 0 Download
AbstractAbstract PDF
An extracellular protease of Salmonella schottmulleri was purified from culture filtrate by using 0-75% ammonium sulfate precipitation, DEAE Sepharose Fast Flow ion exchange chromatography, Ultrogel HA chromatography and Sephacryl S-200 HR molecular sieve chromatography. To measure enzyme activity, synthetic dipeptide substrate (CBZ-arg-arg-AFC) with low molecular weight was employed as substrate. The molecular weight of the purified enzyme was approximately 80 kDa when determined by gel filtration on Sephacryl S-200 HR and 73 kDa when estimated by SDS-PAGE. The isoelectric point was 5.45. The activity of the purified enzyme was inhibited by metal chelating agesnts such as EDTA and 1.10-phenanthroline. The divalent cations, such as Ca^2+, Zn^2+, Fe^2+, Mg^2+ enhanced its activity. These results suggested that it was a metalloprotease. It had a narrow pH optimum of 6.5-7.5 with a maximum at pH 7.0 and a temperature optimum of 40℃. It was stable at least for 1 week at 40℃ and maintained its activity for 24 hours at 50℃, but it was rapidly inactivated at 65℃. This protease was shown to be sensitive to sodium 50℃, but it was rapidly inactivated at 65℃. This protease was shown to be sensitive to sodium 50℃, but it was rapidly inactivated at 65℃. This protease was shown to be sensitive to sodium 50℃, but it was rapidly inactivated at 65℃. This protease was shown to be sensitive to sodium dodecyl sulfate (SDS) and was inactivated in a dose-dependent manner. However, it was resistant to Triton X-100 and the activity was enhanced to 32.3% with treatment of 0.025% Triton X-100.
Characteristics of trypsin-like protease and metalloprotease associated with mycelium differentiation of streptomyces albidoflavus SMF301
Kang, Sung Gyun , Kim, In Seop , Jeong, Byung Cheol , Ryu, Jae Gon , Rho, Yong Taik , Lee, Kye Joon
J. Microbiol. 1995;33(4):307-314.
  • 232 View
  • 0 Download
AbstractAbstract PDF
Trypsin like protease (TLP) and metalloprotease (MTP) were induced in associated with the mycelium differentiation in Streptomyces albidoflavus SMF301. TLP and MTP were purified and characterized from the culture. The molecular mass of TLP and MTP were estimated to be 32 kDa and 18 kDa, respectively. The molecular mass of TLP and MTP were estimated to be 32 kDa and 18 kDa, respectively. The optimum pH and temperature of TLP were 10 and 40℃. Those of MTP were 8 and 55 ℃. TLP was stable at alkaline pH (6-9) and unstable above 45℃ and MTP was stable at alkaline pH and unstable above 80℃. Km and Vmax values with benzoyl-arginyl p-nitroanilide of TLP were 139 uM, and 10 nmole of nitroanilide released per min per ㎍ protein, respectively. Km, and Vmax values with a synthetic substrate, leucine p-nitroanilide, or MTP were 58.9 uM, 3.47 nmol of nitroanilide released per min per/㎍ protein, respectively. TLP was inhibited competitively by leupeptin; the inhibition constant was 0.0031 uM. MTP was inhibited by EDTA, phenonthroline and bestatin.
Physiological importance of trypsin-like protease during morphological differentiation of streptomycetes
Kim, In Seop , Kang, Sung Gyun , Lee, Kye Joon
J. Microbiol. 1995;33(4):315-321.
  • 225 View
  • 0 Download
AbstractAbstract PDF
The relationship between morphological differentiation and production of trypsin-like protease (TLP_ in streptomycetes was studied. All the Streptomyces spp. In this study produced TLP just before the onset of aerial mycelium formation. Addition of TLP inhibitor, TLCK, to the top surface of colonies inhibited aerial mycelium formation as well as TLP inhibitor, TLCK, to the top surface of colonies inhibited aerial mycelium formation as well as TLP activity. Addition of 2% glucose to the Bennett agar medium repressed both the aerial mycelium formation and TLP production in S. abuvaviensis, S. coelicolor A3(2), S exfoliatus, S. microflavus, S. roseus, s. lavendulae, and S. rochei. However the addition of glucose did not affect S. limosus, S. felleus, S. griseus, S. phaechromogenes, and S. rimosus. The glucose repression on aerial mycelium formation and production of TLP was relieved by the addition of glucose anti-metabolite (methyl α-glucopyranoside). Therefore, it was concluded that TLP production is coordinately regulated with morphological differentiation and TLP activity is essential for morphological differentiation in streptomycetes. The proposed role of TLP is that TLP participates in the degradation of substrate mycelium protein for providing nutrient for aerial mycelial growth.
Cloning of the gense coding for extracellular proteases from alkalophilic xanthomonas SP. JK311
Kim, Young Hun , Jang, Ji Yeon , Yeeh, Yeehn , Kim, Yong Ho , Kim, Sang Hae
J. Microbiol. 1995;33(4):344-349.
  • 239 View
  • 0 Download
AbstractAbstract PDF
The alkalophilic bacterium, Xanthomonas sp. JK311, producing extracellular proteases, was isolated from soil. Xanthomonas sp. JK311 produced five extracellular proteases that are all metalloproteases. Four of them were resistant against 1% SDS. Chromosomal DNA of the Xanthomonas sp. JK311 was digested with BamHI and cloned into PUC19. Among E. coli strain HB101 transformants, a clone secreting the proteases was screened through halo formation on skim-milk agar plate and by Southern blot analysis. It had the recombinant plasmid pXEP-1 containing the 7.5 kb-BamHI DNA fragment and produced three extacellular proteases. Their protease properties corresponded to those of Xanthomonas sp. JK311.
Cloning and mulecular characterization of a nprX gene of bacillus subtilis NS15-4 encoding a neutral protease
Lee, Seung Hwan , Yoon, Ki Hong , Nam, Hee Sop , Oh, Tae Kwang , Lee, Seog Jae , Chae, Keon Sang
J. Microbiol. 1996;34(1):68-73.
  • 192 View
  • 0 Download
AbstractAbstract PDF
An nprX gene of Bacillus subtilis NS15-4 encoding a neutral protease was cloned and its molecular characteristics were analyzed. The complete nucleotide sequence indicated that there is an open reading frame (0RF) possibly encoding 521 amino acid polypeptide. The ORF used all codons expected two cysteine and a proline having a codon bias index (CBI) of 0.09 in Escherichia coli. There were homologous sequences to the consensus sequence of -35 and -10 regions of E. coli promoters and to a Shine-Dalgarno (SD) sequence located 25 bp downstream of a major transcription initiation site. Moreover, there were also five minor transcription initiation sites at 6. 7. 8. 14 and 15 nt downstream of the major site. Northern blot analysis revealed the presence of about 1.8 kb mRNA transcript in E. coli having the nprX gene. The nucleotide sequence was identified in GenBank to be a gene for a neutral protease of B. subtilis with six nucleotide difference in the ORF region. The flanking regions of the NprX ORF showed much more differences form those of other neutral protease genes except the nprE gene of B. subtilis, which has the most homology to the nprX gene, and of which the flanking regions were identical to those of the nprX gene.
Degradation of collagens, immunoglobulins, and other serum proteins by protease of salmonella schottmulleri and its toxicity to cultured cells
Na, Byoung Kuk , Kim, Moon Bo , Song, Chul Yong
J. Microbiol. 1996;34(1):95-100.
  • 219 View
  • 0 Download
AbstractAbstract PDF
The effect of the extracellular protease of Salmonella schottmulleri on human serum constituents such as immunoglobulins, hemoglobin and lysozyme and tissue constituents such as fibronectin and collagens was investigated. This protease degraded collagens (type I and III), fibronectin and serum proteins such as human hemoglobin and lysozyme. Bovine serum albumin was degraded slightly. Thus, the present study suggested the possibility that this protease is not only played an important role in invasion of S. schottmulleri by degrading the constituent proteins such as collagens and fibronectin but also induced complications observed in septicemia and chronic infections by degrading the serum proteins. This protease is also capable of degrading defence-oriented humoral proteins, immunoglobulins (IgG and IgM). Furthermore, it is toxic to HEp-2 cells. These findings clarified the possible role of Salmonella protease as a virulence factor in the pathogenesis of Salmonella infections.
Partial characterization of proteases from culture filtrate of mycobacterium tuberculosis
Na, Byoung Kuk , Song, Chul Yong , Park, Young Kil , Bai, Gill Han , Ki, Sang Jae
J. Microbiol. 1996;34(2):198-205.
  • 1,931 View
  • 0 Download
AbstractAbstract PDF
Two proteases were partially characterized from culture filtrate of Mycobacterium, tuberculosis KIT110. Their molecular weights were approximately 200 and 180 kDa, respectively and they exhibited similar enzymatic characteristics. These enzymes were inhibited significantly by EDTA and to some extent by EGTA. Their activity was enhanced by Ca^2+ and Mg^2+ to some degree. However, Cu^2+ and Ag^2+ completely inhibited the enzyme activity at the concentration of 2.5 and 5 mM, respectively. The optimal pH was 7.0 and optimal temperature was around 40℃. These enzymes were rapidly inactivated at 80℃. Therefore, they were heat-labile, neutral metalloproteases. These enzymes exhibited antigenicity shown by their reacting with sera from the partients with pulmonary tuberculosis. These enzymes were able to degrade serum proteins including hemoglobin, bovine serum albumin, lysozyme and immunoglobulin G and structural matrix protein such as type I collagen. Therefore, these enzymes may be thought to contribute to tissue necrosis and pathogenesis during infection.
Expression of Human Protease Inhibitor Nexin-I in Escherichia coli
Ha, Sang Deuk , Kim, Ji Ha , Park, Hey Lyoun , Hyun, Hyung Hwan , Chung, Hyung Min , Kim Kwon, Yun Hee , Seo, Seong Yum , Ko, Jung Jae , Lee, Hyun Hwan
J. Microbiol. 1998;36(4):283-288.
  • 283 View
  • 0 Download
AbstractAbstract PDF
Human protease inhibitor nexin-I(NX-I) cDNA(1.2Kb) was isolated from human lung cDNA library and expressed under the control of T7 promoter as a fused protein in Escherichia coli BL21 and E. coli GJ1158 by addition of IPTG and Nacl as inducers. For GJ1158, 300 mM NaCl was added for induction after the cell reached A_600=0.6. As a result, E. coli GJ1158 showed higher expression level than BL2l with lesser extent of inclusion bodies. The optimum concentration of NaCl exerting no induction effect but shortening the time to reach A_600=0.6 was 50 mM. All the results suggested that E. coli GJ1158 was a useful host for efficient expression of NX-I using NaCl as an inducer. The expressed NX-1 showed an inhibitory effect on thrombin activity. The expressed protein was purified by immobilized metal affinity column chromatography (IMAC) and characterized by digestion with enterokinase (EK).
Purification and Partial Characterization of a metalloprotease in Flammulina velutipes
Shin, Hyun Hee , Choi, Hye Seon
J. Microbiol. 1998;36(1):20-25.
  • 233 View
  • 0 Download
AbstractAbstract PDF
Metalloprotease was detected in the fruit body of the edible mushroom Flammulina velutipe. Inactivation of the metalloprotease reduced mycelial growth signicantly, implying that metalliprotease is important for growth. A neutral metalloprotease was purified by hydrophobic, gel filtration, and anion exchange chromatography. The M_r of the protein was determined to be 30,000 by SDS-PAGE and 33,000 by gel filtration on a Sepjadex G-150 column, indicating that it is a monomer. Its first 11 N-terminal amino acids (P-Q-V-K-T-W-D-L-A) did not show any homology with any known protein in Database(GENEBANK, Swissprot). The enzyme was inhibited by EDTA, 1, 10-phenanthroline, and phosphoamidon but not by inhibitors specific for serine, aspartate and custeine protease. Addition of Zn^2+ and Co^2+ reversed the inhibition caused by 1,10-ohenanthroline. This protease hydrolyzed human fivrinogen, fibrin, azoalbumin, and azocasein as substrates. It showed cleavage preference for hydrophobic residues among tested synthetic substrates.
Characterization of Bacillus cereus SH-7 Extracellular Protease
Hak Kyu Yi , Young Jin Chum , Han Bok Kim
J. Microbiol. 1999;37(4):213-217.
  • 258 View
  • 0 Download
AbstractAbstract PDF
An extracellular endopeptidase from Bacillus cereus SH-7 was purified to homogeneity. The protease was most active at pH 8 and 40 C, respectively. The molecular mass of the protease was 40 kDa on SDS-PAGE, and 120 kDa by gel filtration, suggesting that the native enzyme is composed of three homogeneous subunits. The K_m and V_max values of the protease for N-succinyl-(Ala)_2-Pro-Phe-p-nitroanilide were 11.11 mM and 170 nmol/mg of protein/min, respectively. The protease was also identified as a metalloprotease. The bioactivity of the SH-7 protease will need further study in the future.
Purification and Characterization of Two Extracellular Proteases from Oligotropha carboxydovorans DSM 1227
Kang, Beom Sik , Jeon, Sang Jun , Kim, Min Young
J. Microbiol. 1999;37(1):14-20.
  • 210 View
  • 0 Download
AbstractAbstract PDF
Two extracellular proteases, EP I and EP II, from cells of Oligotropha carboxydovorans (formerly Pseudomonas carboxydovorans) DSM 1227 grown in nutrient broth were purified to greater than 95% homogeneity in five steps using azocasein as a substrate. The final specific activities of EPs I and II were 214.9 and 667.4 units per mg of protein. The molecular weights of native EPs I and II were determined to be 23,000. Sodium dodecyl sulfate-gel electrophoresis revealed the two enzymes to be monomers. The enzymes were found to be serine-type proteases. The activity of EP I was stimulated by Ca^2+, Mg^2+, and Ba^2+, but that of EP II was not. The enzymes were completely inhibited by Fe^2+, Hg^2+, Co^2+, Zn^2+, and Cd^2+. EDTA and EGTA exhibited a strong inhibitory effect on EP I. The optimal pH for the two enzymes was pH 9.0. The optimal temperatures for EP I and II were 60 and 50℃, respectively. The enzymes were stable under alkaline conditions. The thermal stability of EP I was higher than that of EP II. Cell-free extracts did not inhibit the purified enzymes. The enzymes were active on casein, azocasein, azocoll, and carbon monoxide dehydrogenase, but weakly active with bovine serum albumin.
Streptomyces griseus HH1, An A-factor Deficient Mutant, Produces Diminished Level of Trypsin and Increased Level of Metalloproteases
Jung-Mee Kim , Soon-Kwang Hong
J. Microbiol. 2000;38(3):160-168.
  • 207 View
  • 0 Download
AbstractAbstract PDF
A-factor is a microbial hormone that can positively control cell differentiation leading to spore formation and secondary metabolite formation in Streptomyces griseus. To identify a protease that is deeply involved in the morphological and physiological differentiation of Streptomyces, the proteases produced by S. griseus IFO 13350 and its A-factor deficient mutant strain, S. griseus HH1, as well as S. griseus HH1 transformed with the afsA gene were studied. In general, S. griseus showed a higher degree of cell growth and protease activity in proportion to its ability to produce a higher amount of A-factor. In particular, the specific activity of the trypsin of S. griseus IFO 13350 was greatly enhanced more than twice compared with that of S. griseus HH1 in the later stage of growth. The specific activity of the metalloprotease of S. griseus HH1 was greatly enhanced more than twice compared with that of S. griseus IFO 13350, and this observation was reversed in the presence of thiostreptone. However, S. griseus HH1 transformed with the afsA gene showed a significantly decreased level of trypsin and metalloprotease activity compared with that of the HH1 strain. There was no significant difference between S. griseus IFO 13350 and HH1 strain in their chymotrypsin and thiol protease activity, yet the level of leu-aminopeptidase activity was 2 times higher in S. griseus HH1 than in strain IFO 13350. S. griseus HH1 harboring afsA showed a similar level of enzyme activity, however, all the three protease activities sharply increased and the thiol protease activity was critically increased at the end of the fermentation. When a serine protease inhibitor, pefabloc SC, and metalloprotease inhibitor, EDTA, were applied to strain IFO 13350 to examine the in vivo effects of the protease inhibitors on the morphological differentiation, the formation of aerial mycelium and spores was delayed by two or three days.
Controlled Expression and Secretion of Aspergillus oryzae Alkaline Protease in Aspergillus nidulans
Eun Ah Kim , Jeong Goo Lee , Mi Kyung Whang , Hee Moon Park , Jeong Yoon Kim , Suhn Kee Chae , Pil Jae Maeng
J. Microbiol. 2001;39(2):95-101.
  • 247 View
  • 0 Download
AbstractAbstract PDF
In an effort to develop an efficient expression and secretion system for heterologous proteins in Aspergillus nidulans, the PCR-amplified coding sequence for alkaline protease (AlpA) of A. oryzae was cloned into a fungal expression vector downstream of A. nidulans alcA (alcohol dehydrogenase) promoter to yield pRAAlp. Transformation of A. nidulans with pRAAlp gave stable transformants harboring various copy numbers (3 to 10) of integrated alpA gene, from among which 6 representatives were selected. On a medium containing 0.8% ammonium sulfate that represses the expression of the hosts own protease, the alcA promoter-controlled AlpA expression was strongly induced by threonine but repressed by glucose. The level of AlpA secretion was highest (approximately 666 mU/ml) in transformant ALP6 containing the largest copy number integrated alpA. However, the level of AlpA secretion was not necessarily proportional to the copy numbers of the integrated alpA genes. The N-terminal sequence of the secreted mature AlpA was determined to be Gly-Leu-Thr-Thr-Gln-Lys-Ser and its molecular mass to be approximately 34 kDa, indicating that AlpA is properly processed by the removal of 121 N-terminal amino acids.
Overexpression of the sprD Gene Encoding Streptomyces griseus Protease D Stimulates Actinorhodin Production in Streptomyces lividans
Si-Sun Choi , Won-Jae Chi , Jae Hag Lee , Sang-Soon Kang , Byeong Chul Jeong , Soon-Kwang Hong
J. Microbiol. 2001;39(4):305-313.
  • 251 View
  • 0 Download
AbstractAbstract PDF
The sprD gene encoding Streptomyces griseus protease D (SGPD), a chymotrypsin-like protease, was cloned from Streptomyces griseus IFO13350 and sequenced. Most of the amino-acid sequence deduced from the nucleotide sequence is identical to that of Streptomyces griseus IMRU3499 except that one amino acid has been deleted and Trp369 has been substituted into Cys369 in the SGPD from S. griseus IFO13350 without affecting the protease activity. The sprD gene was overexpressed in Streptomyces lividans TK24 as a heterologous host. Various media with different compositions were also used to maximize the productivity of SGPD in the heterologous host. The SGPD productivity was best when the transformant of S. lividans TK24 was cultivated in R2YE medium. The relative chymotrypsin activity of the culture broth measured with an artificial chromogenic substrate, N-succinyl-ala-ala-pro-phe-[rho]-nitroanilide, was 16 units/ml. A high level of SGPD was also produced in YEME and SAAM media but it was relatively lower than in R2YE medium, and negligible amounts of SGPD were produced in GYE, GAE and Benedict media. The growth of S. lividans reached the maximum level of cell mass at days 3 and 4 of the culture, but SGPD production started in the stationary phase of cell growth and kept increasing till the 10th day of culture in R2YE and YEME medium, but in GYE media the productivity reached maximum level at 8 days of cultivation. The introduction of the sprD gene into S. lividans TK24 triggered biosynthesis of the pigmented antibiotic, actinorhodin, which implies some protease may play a very important role in secondary-metabolite formation in Streptomyces.
Purification and Characterization of Caseinolytic Extracellular protease from Bacillus amyloliquefaciens S94
Eui-Sun Son , Jong-Il Kim
J. Microbiol. 2002;40(1):26-32.
  • 211 View
  • 0 Download
AbstractAbstract PDF
From the culture supernatant of the psychrotrophic strain of Bacillus amyloliquefaciens an extracellular serine protease was purified to apparent homogeneity by successive purification steps using QAE-Sephadex, SP-Sephadex and Sephacryl S-100 column chromatography. The protease is monomeric, with a relative molecular mass of 23,000. It is inhibited by the serine protease inhibitor phenylmethylsulfonyl fluoride, but not by EDTA. The enzyme is most active at pH 9-10, and at 45 C, although it is unstable at 60 C.
Multicatalytic Alkaline Serine Protease from the Psychrotrophic Bacillus amyloliquefaciens S94
Eui-Sun Son , Jong-Il Kim
J. Microbiol. 2003;41(1):58-62.
  • 193 View
  • 0 Download
AbstractAbstract PDF
An extracellular protease of Bacillus amyloliquefaciens S94 was purified to apparent homogeneity. The enzyme activity was strongly inhibited by general inhibitor for serine protease, PMSF, suggesting that the enzyme is a serine protease. The purified enzyme activity was inhibited by leucine peptidase inhibitor, bestatin, suggesting that the enzyme is a leucine endopeptidase. The maximum proteolytic activity against different protein substrates occurred at pH 10, 45℃ (protein substrate) and pH 8, 45℃ (synthetic substrate). The purified enzyme was specific in that it readily hydrolyzed substrates with Leu or Lys residues at P1 site. The protease had characteristics of a cold-adapted protein, which was more active for the hydrolysis of synthetic substrate in the range of 15℃ to 45℃, specially at low temperature.
Purification and Characterization of Extracellular Temperature-Stable Serine Protease from Aeromonas hydrophila
Soo-Jin Cho , Jong-Ho Park , Seong Joo Park , Jong-Soon Lim , Eung Ho Kim , Yeon-Jae Cho , Kwang-Soo Shin
J. Microbiol. 2003;41(3):207-211.
  • 221 View
  • 0 Download
AbstractAbstract PDF
Extracellular protease, from Aeromonas hydrophila Ni 39, was purified 16.7-fold to electrophoretic homogeneity with an overall yield of 19.9%, through a purification procedure of acetone precipitation, and Q Sepharose and Sephacryl S-200 chromatographies. The isoelectric point of the enzyme was 6.0 and the molecular mass, as determined by Sephacryl S-200 HR chromatography, was found to be about 102 kDa. SDS/PAGE revealed that the enzyme consisted of two subunits, with molecular masses of 65.9 kDa. Under standard assay conditions, the apparent K_m value of the enzyme toward casein was 0.32 mg/ml. About 90% of the proteolytic activity remained after heating at 60 ℃ for 30 min. The highest rate of azocasein hydrolysis for the enzyme was reached at 60℃, and the optimum pH of the enzyme was 9.0. The enzyme was inhibited by the serine protease inhibitor, phenylmethylsulfonyl fluoride (PMSF), by about 87.9%, but not by E64, EDTA, pepstatin or 1,10-phenanthroline. The enzyme activity was inhibited slightly by Ca_2^+, Mg_2^+ and Zn_2^+ ions.
Journal of Microbiology : Journal of Microbiology
© The Microbiological Society of Korea.
TOP