Journal of Microbiology

Journal Articles

Comparative Secretory Efficiency of Two Chitosanase Signal Peptides from Bacillus subtilis in Escherichia coli: Tae-Yang Eom, Yehui Gang, Youngdeuk Lee, Yoon-Hyeok Kang, Eunyoung Jo, Svini Dileepa Marasinghe, Heung Sik Park, Gun-Hoo Park, Chulhong Oh; J. Microbiol. 2024;62(12):1155-1164. Published online November 25, 2024; DOI: https://doi.org/10.1007/s12275-024-00186-1

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Abstract: The production of recombinant proteins in Escherichia coli is often challenged by cytoplasmic expression due to proteolytic degradation and inclusion body formation. Extracellular expression can overcome these problems by simplifying downstream processing and improving protein yields. This study aims to compare the efficiency of two Bacillus subtilis chitosanase signal peptides in mediating extracellular secretion in E. coli. We identified a naturally occurring mutant signal peptide (mCsn2-SP) from B. subtilis CH2 chitosanase (CH2CSN), which is characterized by a deletion of six amino acids in the N-region relative to the signal peptide (Csn1-SP) from B. subtilis CH1 chitosanase (CH1CSN). The CH1CSN and CH2CSN genes were cloned into the pET-11a vector and protein secretion was evaluated in E. coli BL21(DE3) host cells. Expression was induced with 0.1 mM and 1 mM isopropyl β-D-1-thiogalactopyranoside (IPTG) at 30 °C for one and three days. CH2CSN showed higher secretion levels compared to CH1CSN under all experimental conditions, especially with 0.1 mM IPTG induction for 3 days, which resulted in a 2.37-fold increase in secretion. Furthermore, it was demonstrated that mCsn2-SP is capable of secreting human Cu,Zn-superoxide dismutase (hSOD) in E. coli BL21(DE3) and successfully translocating it to the periplasmic region. This study represents the inaugural investigation into the utilisation of a naturally modified signal peptide, thereby corroborating the assertion that signal peptide deletion variants can influence protein secretion efficiency. Furthermore, the findings substantiate the proposition that such variants can serve as a viable alternative for the secretion of heterologous proteins in E. coli.

Development of a Novel D‑Lactic Acid Production Platform Based on Lactobacillus saerimneri TBRC 5746: Kitisak Sansatchanon , Pipat Sudying , Peerada Promdonkoy , Yutthana Kingcha , Wonnop Visessanguan , Sutipa Tanapongpipat , Weerawat Runguphan , Kanokarn Kocharin; J. Microbiol. 2023;61(9):853-863. Published online September 14, 2023; DOI: https://doi.org/10.1007/s12275-023-00077-x

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D-Lactic acid is a chiral, three-carbon organic acid, that bolsters the thermostability of polylactic acid. In this study, we developed a microbial production platform for the high-titer production of D-lactic acid. We screened 600 isolates of lactic acid bacteria (LAB) and identified twelve strains that exclusively produced D-lactic acid in high titers. Of these strains, Lactobacillus saerimneri TBRC 5746 was selected for further development because of its homofermentative metabolism. We investigated the effects of high temperature and the use of cheap, renewable carbon sources on lactic acid production and observed a titer of 99.4 g/L and a yield of 0.90 g/g glucose (90% of the theoretical yield). However, we also observed L-lactic acid production, which reduced the product’s optical purity. We then used CRISPR/dCas9-assisted transcriptional repression to repress the two Lldh genes in the genome of L. saerimneri TBRC 5746, resulting in a 38% increase in D-lactic acid production and an improvement in optical purity. This is the first demonstration of CRISPR/dCas9-assisted transcriptional repression in this microbial host and represents progress toward efficient microbial production of D-lactic acid.

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Industrial–scale production of various bio–commodities by engineered microbial cell factories: Strategies of engineering in microbial robustness
Ju-Hyeong Jung, Vinoth Kumar Ponnusamy, Gopalakrishnan Kumar, Bartłomiej Igliński, Vinod Kumar, Grzegorz Piechota
Chemical Engineering Journal.2024; 502: 157679. CrossRef
Microbial Cell Factories: Biodiversity, Pathway Construction, Robustness, and Industrial Applicability
Rida Chaudhary, Ali Nawaz, Mireille Fouillaud, Laurent Dufossé, Ikram ul Haq, Hamid Mukhtar
Microbiology Research.2024; 15(1): 247. CrossRef
Adaptive Evolution for the Efficient Production of High-Quality d-Lactic Acid Using Engineered Klebsiella pneumoniae
Bo Jiang, Jiezheng Liu, Jingnan Wang, Guang Zhao, Zhe Zhao
Microorganisms.2024; 12(6): 1167. CrossRef
Enhancing D-lactic acid production from non-detoxified corn stover hydrolysate via innovative F127-IEA hydrogel-mediated immobilization of Lactobacillus bulgaricus T15
Yuhan Zheng, Feiyang Sun, Siyi Liu, Gang Wang, Huan Chen, Yongxin Guo, Xiufeng Wang, Maia Lia Escobar Bonora, Sitong Zhang, Yanli Li, Guang Chen
Frontiers in Microbiology.2024;[Epub] CrossRef

Analysis of a bac operon-silenced strain suggests pleiotropic effects of bacilysin in Bacillus subtilis: Ozan Ertekin , Meltem Kutnu , Aslı Aras Ta&# , Mustafa Demir , Ayten Yazgan Karata&# , Gülay Özcengiz; J. Microbiol. 2020;58(4):297-313. Published online January 28, 2020; DOI: https://doi.org/10.1007/s12275-020-9064-0

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Abstract

Bacilysin, as the simplest peptide antibiotic made up of only L-alanine and L-anticapsin, is produced and excreted by Bacillus subtilis under the control of quorum sensing. We analyzed bacilysin-nonproducing strain OGU1 which was obtained by bacA-targeted pMutin T3 insertion into the parental strain genome resulting in a genomic organization (bacA􍿁::lacZ::erm::bacABCDEF) to form an IPTG-inducible bac operon. Although IPTG induction provided 3- to 5-fold increment in the transcription of bac operon genes, no bacilysin activity was detectable in bioassays and inability of the OGU1 to form bacilysin was confirmed by UPLC-mass spectrometry analysis. Phenotypic analyses revealed the deficiencies in OGU1 with respect to colony pigmentation, spore coat proteins, spore resistance and germination, which could be rescued by external addition of bacilysin concentrate into its cultures. 2DE MALDI-TOF/MS and nanoLC-MS/MS were used as complementary approaches to compare cytosolic proteomes of OGU1. 2-DE identified 159 differentially expressed proteins corresponding to 121 distinct ORFs. In nanoLCMS/ MS, 76 proteins were differentially expressed in OGU1. Quantitative transcript analyses of selected genes validated the proteomic findings. Overall, the results pointed to the impact of bacilysin on expression of certain proteins of sporulation and morphogenesis; the members of mother cell compartment- specific σE and σK regulons in particular, quorum sensing and two component-global regulatory systems, peptide transport, stress response as well as CodY- and ScoCregulated proteins.

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Biocontrol Ability of Strain Bacillus amyloliquefaciens SQ-2 against Table Grape Rot Caused by Aspergillus tubingensis
Suran Li, Shuangshuang Dai, Lei Huang, Yumeng Cui, Ming Ying
Journal of Agricultural and Food Chemistry.2024; 72(44): 24374. CrossRef
Isolation and identification of a novel Bacillus velezensis strain JIN4 and its potential for biocontrol of kiwifruit bacterial canker caused by Pseudomonas syringae pv. actinidiae
Xin Zhao, Yang Zhai, Lin Wei, Fei Xia, Yuanru Yang, Yongjian Yi, Hongying Wang, Caisheng Qiu, Feng Wang, Liangbin Zeng
Frontiers in Plant Science.2024;[Epub] CrossRef
Signatures of kin selection in a natural population of the bacteria Bacillus subtilis
Laurence J Belcher, Anna E Dewar, Chunhui Hao, Melanie Ghoul, Stuart A West
Evolution Letters.2023; 7(5): 315. CrossRef
Comparative biological network analysis for differentially expressed proteins as a function of bacilysin biosynthesis in Bacillus subtilis
Meltem Kutnu, Elif Tekin İşlerel, Nurcan Tunçbağ, Gülay Özcengiz
Integrative Biology.2022; 14(5): 99. CrossRef
Probiotic effects of the Bacillus velezensis GY65 strain in the mandarin fish, Siniperca chuatsi
Jiachuan Wang, Defeng Zhang, Yajun Wang, Zhijun Liu, Lijuan Liu, Cunbin Shi
Aquaculture Reports.2021; 21: 100902. CrossRef
Bacilysin within the Bacillus subtilis group: gene prevalence versus antagonistic activity against Gram-negative foodborne pathogens
Catherine Nannan, Huong Quynh Vu, Annika Gillis, Simon Caulier, Thuy Thanh Thi Nguyen, Jacques Mahillon
Journal of Biotechnology.2021; 327: 28. CrossRef
Impact of spatial proximity on territoriality among human skin bacteria
Jhonatan A. Hernandez-Valdes, Lu Zhou, Marcel P. de Vries, Oscar P. Kuipers
npj Biofilms and Microbiomes.2020;[Epub] CrossRef

Morphologies and phenotypes in Bacillus subtilis biofilms: Xiaoling Wang , Shuo Meng , Jingshi Han; J. Microbiol. 2017;55(8):619-627. Published online July 4, 2017; DOI: https://doi.org/10.1007/s12275-017-7041-z

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Abstract

In this study, we explored Bacillus subtilis biofilm growth under various conditions such as the use of substrates with different stiffnesses and nutrient levels using a well-developed optical imaging technique to spatially and temporally track biofilm growth. We also developed a quantitative method to characterize B. subtilis biofilm morphologies under various growth conditions. To determine biofilm rim irregularities, we used the dimensionless P2A ratio, defined as P2/4πA, where P is the perimeter and A is the area of the biofilm. To estimate biofilm thickness from transmission images, we developed a calibration procedure based on Beer- Lambert’s law and cross sectioning. Furthermore, to determine the distributions of different B. subtilis cell phenotypes during biofilm growth, we used a triple-fluorescence-labeled B. subtilis strain that expressed motility, matrix production, and sporulation. Based on this work, we are able to tune biofilm growth by changing its growing environment.

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Analysis of biofilm expansion rate of Bacillus subtilis (MTC871) on agar substrates with different stiffness
Jin Wu, Xianyong Li, Rui Kong, Jiankun Wang, Xiaoling Wang
Canadian Journal of Microbiology.2023; 69(12): 479. CrossRef
In vitro studies of biofilm-forming Bacillus strains, biocontrol agents isolated from the maize phyllosphere
Aluminé Fessia, Melina Sartori, Daiana García, Luciana Fernández, Rodrigo Ponzio, Germán Barros, Andrea Nesci
Biofilm.2022; 4: 100097. CrossRef
Bistability and Formation of the Biofilm Matrix as Adaptive Mechanisms during the Stationary Phase of Bacillus subtilis
M. R. Sharipova, A. M. Mardanova, N. L. Rudakova, D. S. Pudova
Microbiology.2021; 90(1): 20. CrossRef
Effect of Viscosity on Microswimmers: A Comparative Study
Audrey Nsamela, Priyanka Sharan, Aidee Garcia‐Zintzun, Sandra Heckel, Purnesh Chattopadhyay, Linlin Wang, Martin Wittmann, Thomas Gemming, James Saenz, Juliane Simmchen
ChemNanoMat.2021; 7(9): 1042. CrossRef
Tuning Microbial Activity via Programmatic Alteration of Cell/Substrate Interfaces
Alexey V. Gulyuk, Dennis R. LaJeunesse, Ramon Collazo, Albena Ivanisevic
Advanced Materials.2021;[Epub] CrossRef
Topography and Expansion Patterns at the Biofilm-Agar Interface in Bacillus subtilis Biofilms
Sarah Gingichashvili, Osnat Feuerstein, Doron Steinberg
Microorganisms.2020; 9(1): 84. CrossRef
Applying the handicap principle to biofilms: condition‐dependent signalling inBacillus subtilismicrobial communities
Keith D. Harris, Ilana Kolodkin‐Gal
Environmental Microbiology.2019; 21(2): 531. CrossRef
STUDYING THE INTERNAL STRESS HETEROGENEITY OF THE GROWING BIOFILM BY THE MICROPILLAR DEFORMATION OF THE GROWING SUBSTRATE
XIAOLING WANG, ZHAOCAN WANG, XING SHEN, YUHAO KONG, HUI ZHAO, XIAOQIANG YAN
Journal of Mechanics in Medicine and Biology.2019; 19(06): 1950070. CrossRef

Spectral characterization of a pteridine derivative from cyanide-utilizing bacterium Bacillus subtilis - JN989651: S. Durairaju Nisshanthini , Antony K. Teresa Infanta S. , Duraisamy Senthil Raja , Karuppannan Natarajan , M. Palaniswamy , Jayaraman Angayarkanni; J. Microbiol. 2015;53(4):262-271. Published online March 4, 2015; DOI: https://doi.org/10.1007/s12275-015-4138-0

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Abstract

Soil and water samples were collected from various regions of SIPCOT and nearby Vanappadi Lake, Ranipet, Tamilnadu, India. Based on their colony morphology and their stability during subculturing, 72 bacteria were isolated, of which 14 isolates were actinomycetes. Preliminary selection was carried out to exploit the ability of the microorganisms to utilize sodium cyanate as nitrogen source. Those organisms that were able to utilize cyanate were subjected to secondary screening viz., utilization of sodium cyanide as the nitrogen source. The oxygenolytic cleavage of cyanide is dependent on cyanide monooxygenase which obligately requires pterin cofactor for its activity. Based on this, the organisms capable of utilizing sodium cyanide were tested for the presence of pterin. Thin layer chromatography (TLC) of the cell extracts using n-butanol: 5 N glacial acetic acid (4:1) revealed that 10 out of 12 organisms that were able to utilize cyanide had the pterin-related blue fluorescent compound in the cell extract. The cell extracts of these 10 organisms were subjected to high performance thin layer chromatography (HPTLC) for further confirmation using a pterin standard. Based on the incubation period, cell biomass yield, peak height and area, strain VPW3 was selected and was identified as Bacillus subtilis. The Rf value of the cell extract was 0.73 which was consistent with the 0.74 Rf value of the pterin standard when scanned at 254 nm. The compound was extracted and purified by preparative High Performance Liquid Chromatography (HPLC). Characterization of the compound was performed by ultraviolet spectrum, fluorescence spectrum, Electrospray Ionization-Mass Spectrometry (ESI-MS), and Nuclear Magnetic Resonance spectroscopy (NMR). The compound is proposed to be 6-propionyl pterin (2-amino-6- propionyl-3H-pteridin-4-one).

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Cyanide Bioremediation by Bacillus subtilis under Alkaline Conditions
César Julio Cáceda Quiroz, Gabriela de Lourdes Fora Quispe, Milena Carpio Mamani, Gisela July Maraza Choque, Elisban Juani Sacari Sacari
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Narges Malmir, Najaf Allahyari Fard, Saeed Aminzadeh, Zahra Moghaddassi-Jahromi, Lukhanyo Mekuto
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Brighter is better: bill fluorescence increases social attraction in a colonial seabird and reveals a potential link with foraging
H. D. Douglas, I. V. Ermakov, W. Gellermann
Behavioral Ecology and Sociobiology.2021;[Epub] CrossRef
Microbial (Enzymatic) Degradation of Cyanide to Produce Pterins as Cofactors
Ramasamy Mahendran, Sabna BS, Murugesan Thandeeswaran, Kiran kG, Muthu Vijayasarathy, Jayaraman Angayarkanni, Gayathri Muthusamy
Current Microbiology.2020; 77(4): 578. CrossRef
Metabolic Processes Preserved as Biosignatures in Iron-Oxidizing Microorganisms: Implications for Biosignature Detection on Mars
Melissa A. Merrill Floyd, Amy J. Williams, Andrej Grubisic, David Emerson
Astrobiology.2019; 19(1): 40. CrossRef
Production and optimization of pterin deaminase from cyanide utilizing bacterium Bacillus cereus AM12
Murugesan Thandeeswaran, Sajitha Bijukumar, Mani Arulkumar, Ramasamy Mahendran, Muthusamy Palaniswamy, Jayaraman Angayarkanni
Biotechnology Research and Innovation.2019; 3(1): 159. CrossRef
Evaluation of Pterin, a Promising Drug Candidate from Cyanide Degrading Bacteria
Ramasamy Mahendran, Murugesan Thandeeswaran, Gopikrishnan Kiran, Mani Arulkumar, K. A. Ayub Nawaz, Jayamanoharan Jabastin, Balraj Janani, Thomas Anto Thomas, Jayaraman Angayarkanni
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Venus' Spectral Signatures and the Potential for Life in the Clouds
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Astrobiology.2018; 18(9): 1181. CrossRef
Analeptic agent from microbes upon cyanide degradation
Thandeeswaran Murugesan, Nisshanthini Durairaj, Mahendran Ramasamy, Karunya Jayaraman, Muthusamy Palaniswamy, Angayarkanni Jayaraman
Applied Microbiology and Biotechnology.2018; 102(4): 1557. CrossRef
Pterin function in bacteria
Nathan Feirer, Clay Fuqua
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Effects of Fengycin from Bacillus subtilis fmbJ on Apoptosis and Necrosis in Rhizopus stolonifer: Qunyong Tang , Xiaomei Bie , Zhaoxin Lu , Fengxia Lv , Yang Tao , Xiaoxu Qu; J. Microbiol. 2014;52(8):675-680. Published online August 1, 2014; DOI: https://doi.org/10.1007/s12275-014-3605-3

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Abstract

The lipopeptide antibiotic fengycin, produced by Bacillus subtilis, strongly inhibits growth of filamentous fungi. In this study, we evaluated the effects of fengycin treatment on apoptosis and necrosis in Rhizopus stolonifer by means of cell staining and epifluorescence microscopy. At fengycin concentrations less than 50 μg/ml, treated fungal cells demonstrated a dose-dependent increase in apoptosis-associated markers compared with the untreated control. These markers included chromatin condensation, reactive oxygen species accumulation, mitochondrial membrane potential depolarization, phosphatidylserine externalization, and the occurrence of DNA strand breaks. These results showed that fungal cells were impaired in a number of important functions and entered apoptosis upon treatment with low concentrations of fengycin. In contrast, high concentrations (>50 μg/ml) induced necrosis, indicating that the fungicidal action of fengycin operates via two modes: apoptosis at low concentrations and necrosis at high concentrations. Additionally, the apoptotic effect that we have shown suggests that lower concentrations of fengycin than previously thought may be effective for food preservation.

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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

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Abstract: 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).

In Vitro Development and Transfer of Resistance to Chlortetracycline in Bacillus subtilis: Menghong Dai , Junjie Lu , Yulian Wang , Zhenli Liu , Zonghui Yuan; J. Microbiol. 2012;50(5):807-812. Published online November 4, 2012; DOI: https://doi.org/10.1007/s12275-012-1454-5

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Abstract: The present criteria and rules controlling the approval of the use of probiotics are limited to antibiotic resistance patterns and the presence of antibiotic resistance genes in bacteria. There is little information available in the literature regarding the risk of the usage of probiotics in the presence of antibiotic pressure. In this study we investigated the development and transfer of antibiotic resistance in Bacillus subtilis selected in vitro by chlortetracycline in a stepwise manner. Bacillus subtilis was exposed to increasing concentrations of chlortetracyclineto induce in vitro resistance to chlortetracycline, and the minimal inhibitory concentrations were determinedfor the mutants. Resistant B. subtilis were conjugated with Escherichia coli NK5449 and Enterococcus faecalis JH2-2 using the filter mating. Three B. subtilis tetracycline resistant mutants (namely, BS-1, BS-2, and BS-3) were derived in vitro. A tetracycline resistant gene, tet (K), was found in the plasmids of BS-1 and BS-2. Three conjugates (BS-1N, BS-2N, and BS-3N) were obtained when the resistant B. subtilis was conjugated with E. coli NK5449. The conjugation frequencies for the BS-1N, BS-2N, and BS-3N conjugates were 4.57×10-7, 1.4×10-7, and 1.3×10-8, respectively. The tet(K) gene was found only in the plasmids of BS-1N. These results indicate that long-term use of probiotics under antibiotic selection pressure could cause antibiotic resistance, and the resistance gene could be transferred to other bacteria. The risk arising from the use of probiotics under antibiotic pressure should be considered in the criteria and rules for the safety assessment of probiotics.

Identification of the Genes Involved in 1-Deoxynojirimycin Synthesis in Bacillus subtilis MORI 3K-85: Kyung-Don Kang , Yong Seok Cho , Ji Hye Song , Young Shik Park , Jae Yeon Lee , Kyo Yeol Hwang , Sang Ki Rhee , Ji Hyung Chung , Ohsuk Kwon , Su-Il Seong; J. Microbiol. 2011;49(3):431-440. Published online June 30, 2011; DOI: https://doi.org/10.1007/s12275-011-1238-3

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Abstract: 1-Deoxynojirimycin (DNJ), a D-glucose analogue with a nitrogen atom substituting for the ring oxygen, is a strong inhibitor of intestinal α-glucosidase. DNJ has several promising biological activities, including its antidiabetic, antitumor, and antiviral activities. Nevertheless, only limited amounts of DNJ are available because it can only be extracted from some higher plants, including the mulberry tree, or purified from the culture broth of several types of soil bacteria, such as Streptomyces sp. and Bacillus sp. In our previous study, a DNJ-producing bacterium, Bacillus subtilis MORI, was isolated from the traditional Korean fermented food Chungkookjang. In the present study, we report the identification of the DNJ biosynthetic genes in B. subtilis MORI 3K-85 strain, a DNJ-overproducing derivate of the B. subtilis MORI strain generated by γ-irradiation. The genomic DNA library of B. subtilis MORI 3K-85 was constructed in Escherichia coli, and clones showing α-glucosidase inhibition activity were selected. After DNA sequencing and a series of subcloning, we were able to identify a putative operon which consists of gabT1, yktc1, and gutB1 genes predicted to encode putative transaminase, phosphatase, and oxidoreductase, respectively. When a recombinant plasmid containing this operon sequence was transformed into an E. coli strain, the resulting transformant was able to produce DNJ into the culture medium. Our results indicate that the gabT1, yktc1, and gutB1 genes are involved in the DNJ biosynthetic pathway in B. subtilis MORI, suggesting the possibility of employing these genes to establish a large-scale microbial DNJ overproduction system through genetic engineering and process optimization.

Biochemical Analysis of a Fibrinolytic Enzyme Purified from Bacillus subtilis Strain A1: Won Sik Yeo , Min Jeong Seo , Min Jeong Kim , Hye Hyeon Lee , Byoung Won Kang , Jeong Uck Park , Yung Hyun Choi , Yong Kee Jeong; J. Microbiol. 2011;49(3):376-380. Published online June 30, 2011; DOI: https://doi.org/10.1007/s12275-011-1165-3

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Abstract: A fibrinolytic enzyme from Bacillus subtilis strain A1 was purified by chromatographic methods, including DEAE Sephadex A-50 column chromatography and Sephadex G-50 column gel filtration. The purified enzyme consisted of a monomeric subunit and was estimated to be approximately 28 kDa in size by SDS-PAGE. The specific activity of the fibrinolytic enzyme was 1632-fold higher than that of the crude enzyme extract. The fibrinolytic activity of the purified enzyme was approximately 0.62 and 1.33 U/ml in plasminogen-free and plasminogen-rich fibrin plates, respectively. Protease inhibitors PMSF, DIFP, chymostatin, and TPCK reduced the fibrinolytic activity of the enzyme to 13.7, 35.7, 15.7, and 23.3%, respectively. This result suggests that the enzyme purified from B. subtilis strain A1 was a chymotrypsin-like serine protease. In addition, the optimum temperature and pH range of the fibrinolytic enzyme were 50°C and 6.0-10.0, respectively. The N-terminal amino acid sequence of the purified enzyme was identified as Q-T-G-G-S-I-I-D-P-I-N-G-Y-N, which was highly distinguished from other known fibrinolytic enzymes. Thus, these results suggest a fibrinolytic enzyme as a novel thrombolytic agent from B. subtilis strain A1.

Characterization, Gene Cloning, and Heterologous Expression of β-Mannanase from a Thermophilic Bacillus subtilis: Pijug Summpunn , Suttidarak Chaijan , Duangnate Isarangkul , Suthep Wiyakrutta , Vithaya Meevootisom; J. Microbiol. 2011;49(1):86-93. Published online March 3, 2011; DOI: https://doi.org/10.1007/s12275-011-0357-1

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Abstract

Bacillus subtilis BCC41051 producing a thermostable β-mannanase was isolated from soybean meal-enriched soil and was unexpectedly found to be thermophilic in nature. The extracellular β-mannanase (ManA) produced was hydrophilic, as it was not precipitated even with ammonium sulfate at 80% saturation. The estimated molecular weight of ManA was 38.0 kDa by SDS-PAGE with a pI value of 5.3. Optimal pH and temperature for mannan-hydrolyzing activity was 7.0 and 60°C, respectively. The enzyme was stable over a pH range of 5.0-11.5, and at temperatures of up to 60°C for 30 min, with more than 80% of its activity retained. ManA was strongly inhibited by Hg2+ (1 mM), but was sensitive to other divalent ions to a lesser degree. The gene of ManA encoded a protein of 362 amino acid residues, with the first 26 residues identified as a signal peptide. High expression of recombinant ManA was achieved in both Escherichia coli BL21 (DE3) (415.18 U/ml) and B. megaterium UNcat (359 U/ml).

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Cloning, Expression, and Characterization of β-mannanase from Bacillus subtilis MAFIC-S11 in Pichia pastoris
Junnan Lv, Yiqun Chen, Honglei Pei, Wenhan Yang, Zhimin Li, Bing Dong, Yunhe Cao
Applied Biochemistry and Biotechnology.2013; 169(8): 2326. CrossRef
Novel low-temperature-active, salt-tolerant and proteases-resistant endo-1,4-β-mannanase from a new Sphingomonas strain
Junpei Zhou, Rui Zhang, Yajie Gao, Junjun Li, Xianghua Tang, Yuelin Mu, Feng Wang, Chao Li, Yanyan Dong, Zunxi Huang
Journal of Bioscience and Bioengineering.2012; 113(5): 568. CrossRef
Mannanases: microbial sources, production, properties and potential biotechnological applications
Prakram Singh Chauhan, Neena Puri, Prince Sharma, Naveen Gupta
Applied Microbiology and Biotechnology.2012; 93(5): 1817. CrossRef

Evaluation of Antagonistic Activities of Bacillus subtilis and Bacillus licheniformis Against Wood-Staining Fungi: In Vitro and In Vivo Experiments: Natarajan Velmurugan , Mi Sook Choi , Sang-Sub Han , Yang-Soo Lee; J. Microbiol. 2009;47(4):385-392. Published online September 9, 2009; DOI: https://doi.org/10.1007/s12275-009-0018-9

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Abstract: The antifungal activity of bacterial strains Bacillus subtilis EF 617317 and B. licheniformis EF 617325 was demonstrated against sapstaining fungal cultures Ophiostoma flexuosum, O. tetropii, O. polonicum, and O. ips in both in vitro and in vivo conditions. The crude active supernatant fractions of 7 days old B. subtilis and B. licheniformis cultures inhibited the growth of sapstaining fungi in laboratory experiments. Thermostability and pH stability of crude supernatants were determined by series of experiments. FT-IR analysis was performed to confirm the surface structural groups of lipoproteins present in the crude active supernatant. Partial purification of lipopeptides present in the crude supernatant was done by using Cellulose anion exchange chromatography and followed by Sephadex gel filtration chromatography. Partially purified compounds significantly inhibited the sapstaining fungal growth by in vitro analysis. The lipopeptides responsible for antifungal activity were identified by electrospray ionization mass spectrometry after partial purification by ion exchange and gel filtration chromatography. Four major ion peaks were identified as m/z 1023, 1038, 1060, and 1081 in B. licheniformis and 3 major ion peaks were identified as m/z 1036, 1058, and 1090 in B. subtilis. In conclusion, the partially purified lipopeptides may belong to surfactin and iturin family. In vivo analysis for antifungal activity of lipopeptides on wood was conducted in laboratory. In addition, the potential of extracts for fungal inhibition on surface and internal part of wood samples were analyzed by scanning electron microscopy.

Journal Article

Characterization of the Bacillus subtilis WL-3 Mannanase from a Recombinant Escherichia coli: Ki-Hong Yoon , Seesub Chung , Byung-Lak Lim; J. Microbiol. 2008;46(3):344-349. Published online July 5, 2008; DOI: https://doi.org/10.1007/s12275-008-0045-y

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Abstract: A mannanase was purified from a cell-free extract of the recombinant Escherichia coli carrying a Bacillus subtilis WL-3 mannanase gene. The molecular mass of the purified mannanase was 38 kDa as estimated by SDS-PAGE. Optimal conditions for the purified enzyme occurred at pH 6.0 and 60°C. The specific activity of the purified mannanase was 5,900 U/mg on locust bean gum (LBG) galactomannan at pH 6.0 and 50°C. The activity of the enzyme was slightly inhibited by Mg2+, Ca2+, EDTA and SDS, and noticeably enhanced by Fe2+. When the enzyme was incubated at 4°C for one day in the presence of 3 mM Fe2+, no residual activity of the mannanase was observed. The enzyme showed higher activity on LBG and konjac glucomannan than on guar gum galactomannan. Furthermore, it could hydrolyze xylans such as arabinoxylan, birchwood xylan and oat spelt xylan, while it did not exhibit any activities towards carboxymethylcellulose and para-nitrophenyl-β-mannopyranoside. The predominant products resulting from the mannanase hydrolysis were mannose, mannobiose and mannotriose for LBG or mannooligosaccharides including mannotriose, mannotetraose, mannopentaose and mannohexaose. The enzyme could hydrolyze mannooligosaccharides larger than mannobiose.

Research Support, Non-U.S. Gov'ts

Sterilization of Bacteria, Yeast, and Bacterial Endospores by Atmospheric-Pressure Cold Plasma using Helium and Oxygen: Kyenam Lee , Kwang-hyun Paek , Won-Tae Ju , Yoenhee Lee; J. Microbiol. 2006;44(3):269-275.; DOI: https://doi.org/2386 [pii]

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Abstract: Atmospheric-pressure cold plasma (APCP) using helium/oxygen was developed and tested as a suitable sterilization method in a clinical environment. The sterilizing effect of this method is not due to UV light, which is known to be the major sterilization factor of APCP, but instead results from the action of reactive oxygen radicals. Escherichia coli, Staphylococcus aureus, and Saccharomyces cerevisiae deposited on a nitrocellulose filter membrane or Bacillus subtilis spores deposited on polypropylene plates were exposed to helium/oxygen plasma generated with AC input power at 10 kHz, 6 kV. After plasma treatment, nitrocellulose filter membranes were overlaid on fresh solid media and CFUs were counted after incubation overnight. D-values were 18 sec for E. coli, 19 sec for S. aureus, 1 min 55 sec for S. cerevisiae, and 14 min for B. subtilis spores. D-values of bacteria and yeast were dependent on the initial inoculation concentration, while the D-value of B. subtilis spores showed no correlation. When treated cells were observed with a scanning electron microscope, E. coli was more heavily damaged than S. aureus, S. cerevisiae exhibited peeling, and B. subtilis spores exhibited shrunken morphology. Results showed that APCP using helium/oxygen has many advantages as a sterilization method, especially in a clinical environment with conditions such as stable temperature, unlimited sample size, and no harmful gas production.

YlaC is an Extracytoplasmic Function (ECF) Sigma Factor Contributing to Hydrogen Peroxide Resistance in Bacillus subtilis: Han-Bong Ryu , Inji Shin , Hyung-Soon Yim , Sa-Ouk Kang; J. Microbiol. 2006;44(2):206-216.; DOI: https://doi.org/2363 [pii]

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Abstract: In this study, we have attempted to characterize the functions of YlaC and YlaD encoded by ylaC and ylaD genes in Bacillus subtilis. The GUS reporter gene, driven by the yla operon promoter, was expressed primarily during the late exponential and early stationary phase, and its expression increased as the result of hydrogen peroxide treatment. Northern and Western blot analyses revealed that the level of ylaC transcripts and YlaC increased as the result of challenge with hydrogen peroxide. A YlaC-overexpressing strain evidenced hydrogen peroxide resistance and a three-fold higher peroxidase activity as compared with a deletion mutant. YlaC-overexpressing and YlaD-disrupted strains evidenced higher sporulation rates than were observed in the YlaC-disrupted and YlaD-overexpressing strains. Analyses of the results of native polyacrylamide gel electrophoresis of recombinant YlaC and YlaD indicated that interaction between YlaC and YlaD was regulated by the redox state of YlaD in vitro. Collectively, the results of this study appear to suggest that YlaC regulated by the YlaD redox state, contribute to oxidative stress resistance in B. subtilis.

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