Journal of Microbiology

Review

High yield strategies for triterpenoid biosynthesis in cell factories: Mingzhu Zheng, Chuang Liu, Ceyuan Liu, Jing Xie, Gen Pan, Can Zhong, Jian Jin; Received September 28, 2025 Accepted February 13, 2026 Published online April 21, 2026; DOI: https://doi.org/10.71150/jm.2509018 [Epub ahead of print]

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Abstract PDF Supplementary Material: Triterpenoids are natural products widely found in the plant kingdom and have various pharmacological effects such as anti-inflammatory, antioxidant and anti-tumour. However, the content of triterpenoids in medicinal plants is low, and it is difficult to purify and isolate them due to their complex structure. The efficient production of some triterpenoids in chassis organisms has been achieved by constructing a heterologous triterpenoid synthesis pathway in engineered strains such as yeast, modifying the key enzymes in the pathway, and adjusting the metabolism of yeast. Modification of key enzymes in the synthetic pathway is currently an effective strategy to enhance the heterologous synthesis of triterpenoids. This paper reviews the current research progress on the modification of key enzymes downstream in the synthetic pathway and the design of key enzymes around them to enhance triterpenoid production in five main areas: 1) increasing the supply of triterpenoid precursors; 2) inhibition of the natural sterol pathway; 3) fusion expression of related enzymes; 4) compartmentalisation of the metabolic pathway; and 5) tapping and enhancing the triterpenoid efflux pump. Finally, recent advances and applications of artificial intelligence (AI) in enzyme engineering and pathway design for triterpenoid biosynthesis are highlighted. Challenges and perspectives for further increasing the yield of triterpenoid synthesis in Saccharomyces cerevisiae are presented.

Articles

In Silico Intensive Analysis for the E4 Gene Evolution of Human Adenovirus Species D: Chanhee Lee, Anyeseu Park, Jeong Yoon Lee; J. Microbiol. 2024;62(5):409-418. Published online April 30, 2024; DOI: https://doi.org/10.1007/s12275-024-00132-1

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Abstract PDF: Adenovirus (Ad) is a ubiquitous pathogen capable of infecting a wide range of animals and humans. Human Adenovirus (HAdV) can cause severe infection, particularly in individuals with compromised immune systems. To date, over 110 types of HAdV have been classified into seven species from A to G, with the majority belonging to the human adenovirus species D (HAdV-D). In the HAdV-D, the most significant factor for the creation of new adenovirus types is homologous recombination between viral genes involved in determining the virus tropism or evading immune system of host cells. The E4 gene, consisting of seven Open Reading Frames (ORFs), plays a role in both the regulation of host cell metabolism and the replication of viral genes. Despite long-term studies, the function of each ORF remains unclear. Based on our updated information, ORF2, ORF3, and ORF4 have been identified as regions with relatively high mutations compared to other ORFs in the E4 gene, through the use of in silico comparative analysis. Additionally, we managed to visualize high mutation sections, previously undetectable at the DNA level, through a powerful amino acid sequence analysis tool known as proteotyping. Our research has revealed the involvement of the E4 gene in the evolution of human adenovirus, and has established accurate sequence information of the E4 gene, laying the groundwork for further research.

Regulatory role of cysteines in (2R, 3R)-butanediol dehydrogenase BdhA of Bacillus velezensis strain GH1-13: Yunhee Choi , Yong-Hak Kim; J. Microbiol. 2022;60(4):411-418. Published online March 14, 2022; DOI: https://doi.org/10.1007/s12275-022-2018-y

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Bacillus velezensis strain GH1-13 contains a (2R,3R)-butanediol dehydrogenase (R-BDH) BdhA which converts acetoin to R-BD reversibly, however, little is known about its regulatory cysteine and biological significance. We performed sitedirected mutation of three cysteines in BdhA. The C37S mutant had no enzyme activity and the C34S and C177S mutants differed from each other and wild type (WT). After zinc affinity chromatography, 1 mM ZnCl2 treatment resulted in a 3-fold enhancement of the WT activity, but reduced activity of the C34S mutant by more than 2 folds compared to the untreated ones. However, ZnCl2 treatment did not affect the activity of the C177S mutant. Most of the double and triple mutant proteins (C34S/C37S, C34S/C177S, C37S/C177S, and C34S/C37S/C177S) were aggregated in zinc resins, likely due to the decreased protein stability. All of the purified WT and single mutant proteins increased multiple intermolecular disulfide bonds in the presence of H2O2 as the buffer pH decreased from 7.5 to 5.5, whereas an intramolecular disulfide bond of cysteine 177 and another cysteine in the CGIC motif region was likely formed at pH higher than pKa of 7.5. When pH varied, WT and its C34S or C177S mutants reduced acetoin to R-BD at the optimum pH 5.5 and oxidized R-BD to acetoin at the optimum pH 10. This study demonstrated that cysteine residues in BdhA play a regulatory role for the production of acetoin and R-BD depending on pH as well as metal binding and oxidative stress.

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Significantly enhanced specific activity of Bacillus subtilis (2,3)-butanediol dehydrogenase through computer-aided refinement of its substrate-binding pocket
Bochun Hu, Xiaoqi Xi, Fugang Xiao, Xiaomeng Bai, Yuanyuan Gong, Yifan Li, Xueqin Qiao, Cunduo Tang, Jihong Huang
International Journal of Biological Macromolecules.2024; 281: 136443. CrossRef
Structural and enzymatic characterization of Bacillus subtilis R,R-2,3-butanediol dehydrogenase
Xiaofei Wang, Lingyun Jia, Fangling Ji
Biochimica et Biophysica Acta (BBA) - General Subjects.2023; 1867(4): 130326. CrossRef
Engineering a BsBDHA substrate-binding pocket entrance for the improvement in catalytic performance toward (R)-phenyl-1,2-ethanediol based on the computer-aided design
Bo-Chun Hu, Meng-Ran Li, Ying-Ying Li, Xin-Shuang Yuan, Yu-Ye Hu, Fu-Gang Xiao
Biochemical Engineering Journal.2023; 194: 108907. CrossRef

Salmonella Typhimurium ST313 isolated in Brazil revealed to be more invasive and inflammatory in murine colon compared to ST19 strains: Amanda Aparecida Seribelli , Tamara R. Machado Ribeiro , Patrick da Silva† , Isabela Mancini Martins , Felipe Pinheiro Vilela , Marta I. Cazentini Medeiros , Kamila Chagas Peronni , Wilson Araújo da Silva Junior , Cristiano Gallina Moreira , Juliana Pfrimer Falcão; J. Microbiol. 2021;59(9):861-870. Published online August 12, 2021; DOI: https://doi.org/10.1007/s12275-021-1082-z

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Salmonella Typhimurium (ST313) has caused an epidemic of invasive disease in sub-Saharan Africa and has been recently identified in Brazil. As the virulence of this ST is poorly understood, the present study aimed to (i) perform the RNAseq in vitro of S. Typhimurium STm30 (ST313) grown in Luria-Bertani medium at 37°C; (ii) compare it with the RNAseq of the S. Typhimurium SL1344 (ST19) and S. Typhimurium STm11 (ST19) strains under the same growing conditions; and (iii) examine the colonization capacity and expression of virulence genes and cytokines in murine colon. The STm30 (ST313) strain exhibited stronger virulence and was associated with a more inflammatory profile than the strains SL1344 (ST19) and STm11 (ST19), as demonstrated by transcriptome and in vivo assay. The expression levels of the hilA, sopD2, pipB, and ssaS virulence genes, other Salmonella pathogenicity islands SPI-1 and SPI-2 genes or effectors, and genes of the cytokines IL-1β, IFN-γ, TNF-α, IL-6, IL-17, IL-22, and IL-12 were increased during ST313 infection in C57BL/6J mice. In conclusion, S. Typhimurium STm30 (ST313) isolated from human feces in Brazil express higher levels of pathogenesis- related genes at 37°C and has stronger colonization and invasion capacity in murine colon due to its high expression levels of virulence genes, when compared with the S. Typhimurium SL1344 (ST19) and STm11 (ST19) strains. STm30 (ST313) also induces stronger expression of pro-inflammatory cytokines in this organ, suggesting that it causes more extensive tissue damage.

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Inflammation, toxicity, and apoptosis reducing potential of bacteriophage Ariobarzanes on intestinal cells infected with Salmonella Typhimurium
Mina Rahiminejad, Maryam Montaseri, Mohammad Hashem Yousefi, Saeed Nazifi, Jeroen Wagemans, Saeid Hosseinzadeh
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Whole-Genome Sequencing Reveals the Population Structure and Genetic Diversity of Salmonella Typhimurium ST34 and ST19 Lineages
Zhen-xu Zhuo, Yu-lian Feng, Xi-wei Zhang, Hao Liu, Fang-yin Zeng, Xiao-yan Li
Journal of Microbiology.2024; 62(10): 859. CrossRef
Incremental increases in physiological fluid shear progressively alter pathogenic phenotypes and gene expression in multidrug resistant Salmonella
Jiseon Yang, Jennifer Barrila, Eric A. Nauman, Seth D. Nydam, Shanshan Yang, Jin Park, Ami D. Gutierrez-Jensen, Christian L. Castro, C. Mark Ott, Kristina Buss, Jason Steel, Anne D. Zakrajsek, Mary M. Schuff, Cheryl A. Nickerson
Gut Microbes.2024;[Epub] CrossRef
Virulence potential of Salmonella 1,4, [5],12:i:- strains isolated during decades from different sources in the Southeast region of Brazil
Giovana do Nascimento Pereira, Amanda Aparecida Seribelli, Carolina Nogueira Gomes, Felipe Pinheiro Vilela, Ludmilla Tonani, Monique Ribeiro Tiba-Casas, Marta Inês Cazentini Medeiros, Dália dos Prazeres Rodrigues, Márcia Regina von Zeska Kress, Juliana Pf
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Invasive non-typhoidal Salmonella (iNTS) aminoglycoside-resistant ST313 isolates feature unique pathogenic mechanisms to reach the bloodstream
Isabela Mancini Martins, Amanda Aparecida Seribelli, Tamara R. Machado Ribeiro, Patrick da Silva, Bruna Cardinali Lustri, Rodrigo T. Hernandes, Juliana Pfrimer Falcão, Cristiano Gallina Moreira
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Regulator of RNase E activity modulates the pathogenicity of Salmonella Typhimurium
Jaejin Lee, Eunkyoung Shin, Ji-Hyun Yeom, Jaeyoung Park, Sunwoo Kim, Minho Lee, Kangseok Lee
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Antimicrobial resistance and genetic background of non-typhoidal Salmonella enterica strains isolated from human infections in São Paulo, Brazil (2000–2019)
Aline Parolin Calarga, Marco Tulio Pardini Gontijo, Luiz Gonzaga Paula de Almeida, Ana Tereza Ribeiro de Vasconcelos, Leandro Costa Nascimento, Taíse Marongio Cotrim de Moraes Barbosa, Thalita Mara de Carvalho Perri, Silvia Regina dos Santos, Monique Ribe
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Antarctic tundra soil metagenome as useful natural resources of cold-active lignocelluolytic enzymes: Han Na Oh , Doyoung Park , Hoon Je Seong , Dockyu Kim , Woo Jun Sul; J. Microbiol. 2019;57(10):865-873. Published online September 30, 2019; DOI: https://doi.org/10.1007/s12275-019-9217-1

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Lignocellulose composed of complex carbohydrates and aromatic heteropolymers is one of the principal materials for the production of renewable biofuels. Lignocellulose-degrading genes from cold-adapted bacteria have a potential to increase the productivity of biological treatment of lignocellulose biomass by providing a broad range of treatment temperatures. Antarctic soil metagenomes allow to access novel genes encoding for the cold-active lignocellulose-degrading enzymes, for biotechnological and industrial applications. Here, we investigated the metagenome targeting cold-adapted microbes in Antarctic organic matter-rich soil (KS 2-1) to mine lignolytic and celluloytic enzymes by performing single molecule, real-time metagenomic (SMRT) sequencing. In the assembled Antarctic metagenomic contigs with relative long reads, we found that 162 (1.42%) of total 11,436 genes were annotated as carbohydrate-active enzymes (CAZy). Actinobacteria, the dominant phylum in this soil’s metagenome, possessed most of candidates of lignocellulose catabolic genes like glycoside hydrolase families (GH13, GH26, and GH5) and auxiliary activity families (AA7 and AA3). The predicted lignocellulose degradation pathways in Antarctic soil metagenome showed synergistic role of various CAZyme harboring bacterial genera including Streptomyces, Streptosporangium, and Amycolatopsis. From phylogenetic relationships with cellular and environmental enzymes, several genes having potential for participating in overall lignocellulose degradation were also found. The results indicated the presence of lignocellulose-degrading bacteria in Antarctic tundra soil and the potential benefits of the lignocelluolytic enzymes as candidates for cold-active enzymes which will be used for the future biofuel-production industry.

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Cross-scale adaptation and biotechnological potential of cold-active bacteria in lignocellulose degradation
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Oxygen-mediated growth enhancement of an obligate anaerobic archaeon Thermococcus onnurineus NA1: Seong Hyuk Lee , Hwan Youn , Sung Gyun Kang , Hyun Sook Lee; J. Microbiol. 2019;57(2):138-142. Published online January 31, 2019; DOI: https://doi.org/10.1007/s12275-019-8592-y

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Thermococcus onnurineus NA1, an obligate anaerobic hyperthermophilic archaeon, showed variable oxygen (O2) sensitivity depending on the types of substrate employed as an energy source. Unexpectedly, the culture with yeast extract as a sole energy source showed enhanced growth by 2-fold in the presence of O2. Genome-wide transcriptome analysis revealed the upregulation of several antioxidant-related genes encoding thioredoxin peroxidase (TON_0862), rubrerythrin (TON_0864), rubrerythrin-related protein (TON_0873), NAD(P)H rubredoxin oxidoreductase (TON_0865), or thioredoxin reductase (TON_1603), which can couple the detoxification of reactive oxygen species with the regeneration of NAD(P)+ from NAD(P)H. We present a plausible mechanism by which O2 serves to maintain the intracellular redox balance. This study demonstrates an unusual strategy of an obligate anaerobe underlying O2-mediated growth enhancement despite not having heme-based or cytochrome-type proteins.

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Exploration of formate as a liquid organic hydrogen carrier in biohydrogen production through evolutionary and process engineering of hyperthermophilic archaeon
Hae-Chang Jung, Sung-Mok Lee, Ji-in Yang, Seong Hyuk Lee, Hyun Sook Lee, Sung Gyun Kang
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Eric Runge, Sara Vulpius, Daniel Herwartz, Andreas Pack, Caroline Brachmann, Lena Noack
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Jasmine S Berg, Soeren Ahmerkamp, Petra Pjevac, Bela Hausmann, Jana Milucka, Marcel M M Kuypers
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Promising cellulolytic fungi isolates for rice straw degradation: Diana Catalina Pedraza-Zapata , Andrea Melissa Sánchez-Garibello , Balkys Quevedo-Hidalgo , Nubia Moreno-Sarmiento , Ivonne Gutiérrez-Rojas; J. Microbiol. 2017;55(9):711-719. Published online September 2, 2017; DOI: https://doi.org/10.1007/s12275-017-6282-1

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The objective of this study was to evaluate the potential of eight fungal isolates obtained from soils in rice crops for straw degradation in situ. From the initial eight isolates, Pleurotus ostreatus T1.1 and Penicillium sp. HC1 were selected for further characterization based on qualitative cellulolytic enzyme production and capacity to use rice straw as a sole carbon source. Subsequently, cellulolytic, xylanolytic, and lignolytic (Pleurotus ostreatus) activity on carboxymethyl cellulose, oat xylan, and rice straw with different nitrogen sources was evaluated. From the results obtained it was concluded both isolates are capable to produce enzymes necessary for rice straw degradation. However, their production is dependent upon carbon and nitrogen source. Last, it was established that Pleurotus ostreatus T1.1 and Penicillium sp. HC1 capability to colonize and mineralize rice straw, in mono-and co-culture, without affecting nitrogen soil content.

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Food Chemistry: X.2026; 33: 103467. CrossRef
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Ayumi Shikata, Junjarus Sermsathanaswadi, Phakhinee Thianheng, Sirilak Baramee, Chakrit Tachaapaikoon, Rattiya Waeonukul, Patthra Pason, Khanok Ratanakhanokchai, Akihiko Kosugi
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Alteration in the ultrastructural morphology of mycelial hyphae and the dynamics of transcriptional activity of lytic enzyme genes during basidiomycete morphogenesis: Elena Vetchinkina , Maria Kupryashina , Vladimir Gorshkov , Marina Ageeva , Yuri Gogolev , Valentina Nikitina; J. Microbiol. 2017;55(4):280-288. Published online January 26, 2017; DOI: https://doi.org/10.1007/s12275-017-6320-z

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The morphogenesis of macromycetes is a complex multilevel process resulting in a set of molecular-genetic, physiological- biochemical, and morphological-ultrastructural changes in the cells. When the xylotrophic basidiomycetes Lentinus edodes, Grifola frondosa, and Ganoderma lucidum were grown on wood waste as the substrate, the ultrastructural morphology of the mycelial hyphal cell walls differed considerably between mycelium and morphostructures. As the macromycetes passed from vegetative to generative development, the expression of the tyr1, tyr2, chi1, chi2, exg1, exg2, and exg3 genes was acti-vated. These genes encode enzymes such as tyrosinase, chi-tinase, and glucanase, which play essential roles in cell wall growth and morphogenesis.

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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

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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.

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Heat Shock Causes Oxidative Stress and Induces a Variety of Cell Rescue Proteins in Saccharomyces cerevisiae KNU5377: Il-Sup Kim , Hye-Youn Moon , Hae-Sun Yun , Ingnyol Jin; J. Microbiol. 2006;44(5):492-501.; DOI: https://doi.org/2449 [pii]

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Abstract PDF: In this study, we attempted to characterize the physiological response to oxidative stress by heat shock in Saccharomyces cerevisiae KNU5377 (KNU5377) that ferments at a temperature of 40°C. The KNU5377 strain evidenced a very similar growth rate at 40°C as was recorded under normal conditions. Unlike the laboratory strains of S. cerevisiae, the cell viability of KNU5377 was affected slightly under 2 hours of heat stress conditions at 43°C. KNU5377 evidenced a time-dependent increase in hydroperoxide levels, carbonyl contents, and malondialdehyde (MDA), which increased in the expression of a variety of cell rescue proteins containing Hsp104p, Ssap, Hsp30p, Sod1p, catalase, glutathione reductase, G6PDH, thioredoxin, thioredoxin peroxidase (Tsa1p), Adhp, Aldp, trehalose and glycogen at high temperature. Pma1/2p, Hsp90p and H+-ATPase expression levels were reduced as the result of exposure to heat shock. With regard to cellular fatty acid composition, levels of unsaturated fatty acids (USFAs) were increased significantly at high temperatures (43°C), and this was particularly true of oleic acid (C18:1). The results of this study indicated that oxidative stress as the result of heat shock may induce a more profound stimulation of trehalose, antioxidant enzymes, and heat shock proteins, as well as an increase in the USFAs ratios. This might contribute to cellular protective functions for the maintenance of cellular homeostasis, and may also contribute to membrane fluidity.

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Safety Assessment of Potential Lactic Acid Bacteria Bifidobacterium longum SPM1205 Isolated from Healthy Koreans: Sung Sook Choi , Byung Yong Kang , Myung Jun Chung , Soo Dong Kim , So Hee Park , Jung Soo Kim , Chin Yang Kang , Nam Joo Ha; J. Microbiol. 2005;43(6):493-498.; DOI: https://doi.org/2300 [pii]

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Abstract PDF: The safety assessment of Bifidobacterium longum SPM1205 isolated from healthy Koreans and this strain''''''''s inhibitory effects on fecal harmful enzymes of intestinal microflora were investigated. The overall safety of this strain was investigated during a feeding trial. Groups of SD rats were orally administered a test strain or commercial reference strain B. longum 1?109 CFU/kg body weight/day for four weeks. Throughout this time, their feed intake, water intake and live body weight were monitored. Fecal samples were periodically collected to test harmful enzyme activities of intestinal microflora. At the end of the four-week observation period, samples of blood, liver, spleen, kidney, and gut tissues were collected to determine for hematological parameters and histological differences. The results obtained in this experiment demonstrated that four weeks of consumption of this Bifidobacterium strain had no adverse effects on rat''''''''s general health status, blood biochemical parameters or histology. Therefore, it is likely to be safe for human use. Fecal harmful enzymes such as -glucosidase, -glucuronidase, tryptophanase and urease, were effectively inhibited during the administration of the B. longum SPM1205. These results suggested that this B. longum SPM 1205 could be used for humans as a probiotic strain.

Purification and Characterization of Catalase-3 of Deinococcus radiophilus: Lee, In Jeong , Lee, Young Nam; J. Microbiol. 1995;33(3):239-243.

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Abstract PDF: Deinococcus radiophilus, an UV resistant bacterium seemed to contain three issoenzymes of catalase. Among them, the samllest and most abundant species in cell-free extract, catalase-3 which also exhibited peroxidase activity was purified to electrophoretic homogeneity (145-fold purification) by chromatographic procedures. Its molecular weight was 155 kDa composed of four 38 kDa subunits. The K_m value of catalase-3 for H₂O₂was approximately 0.5 mM. This enzyme showed a typical ferric heme spectrum with maximum absorption at 405 nm. Upon binding to cyanide, the 405 nm peak shifted to 420 nm. Catalase-3 was very sensitive to inhibitors of heme proteins, such as cyanide, azide and hydroxylamine. A ratio of A_405/A_28O was 0.5 Catalase-3 was active over a wide range of pH, between pH 7 and 10. The enzyme was rather heat-labile and partially sensitive to ethanol-chloroform treatment, but resistant to 3-amino-1, 2, 4-triazole. Catalase-3 of D. radiophilus, which is a bifunction catalatic peroxidatic enzyme seemed to share certain molecular properties with the typical catalase and the catalase-peroxidase along with its own unique features.

Protective Effects of Antoxidant Enzymes of Candida albicans against Oxidative Killing by Macrophages: Kim, Hye Jin , Na, Byoung Kuk , Kim, Moon Bo , Choi, Duk Young , Song, Chul Yong; J. Microbiol. 1999;37(2):117-122.

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Abstract PDF: Protective roles of antioxidant enzymes, copper-zinc superoxide dismutase (CuZnSOD), manganese superoxide dismutase (MnSOD), and catalase of Candida albicans against exogenous reactive oxygens and oxidative killing by macrophages were investigated. The initial growth of C. albicans was inhibited by reactive, oxygen-producing chemicals such as hydrogen peroxide, pyrogallol, and paraquat, but it was restored as the production of antioxidant enzymes were increased. The growth inhibition of C. albicans by reactive, oxygen-producing chemicals was reduced by treating the purified candidal SOD and catalase. Also, in the presence of SOD and catalase, the oxidative killing of C. albicans by macrophages was significantly inhibited. These results suggest that antioxidant enzymes, CuZnSOD, MnSOD, and catalase of C. albicans may play important roles in the protection of C. albicans not only from exogenous oxidative stress but also from oxidative killing by macrophages.

Alterations in the Activities of Antioxidant Enzymes of Human Dermal Microvascular Endothelial Cells Infected with Orientia tsutsugamushi: Young-Sang Koh; J. Microbiol. 2001;39(2):142-145.

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Abstract PDF: Changes in the activities of several antioxidant enzymes in transformed human dermal microvascular endothelial cells (HMEC-1) by infection with the obligate intracellular bacterium Orientia tsutsugamushi, the causative agent of scrub typhus, were investigated. The activities of glucose-6-phosphate dehydrogenase, catalase, and glutathione peroxidase were significantly decreased in HMEC-1 cells infected with O. tsutsugamushi. However, the level of superoxide dismutase increased slightly. Furthermore, increased levels of intracellular peroxide was observed in HMEC-1 during infection. These results support the hypothesis that cells infected by this intracellular bacterium experience oxidant-mediated injury that may eventually contribute to cell death.

Comparative Enzyme Production by Fungi from Diverse Lignocellulosic Substrates: Marie K. W. Sin , Kevin D. Hyde , Stephen B. Pointing; J. Microbiol. 2002;40(3):241-244.

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Abstract PDF: Fungi commonly encountered on monocotyledonous substrates were evaluated for their in vitro ability to produce enzymes involved in lignocellulose breakdown. Most were capable of structural polysaccharide utilization, but few produced enzymes associated with lignin breakdown. None of the monocotyledon-inhabiting fungi produced reactions as strongly as wood decay fungi.

Quorum Sensing and Quorum-Quenching Enzymes: Yi-Hu Dong , Lian-Hui Zhang; J. Microbiol. 2005;43(1):101-109.

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Abstract PDF: To gain maximal benefit in a competitive environment, single-celled bacteria have adopted a community genetic regulatory mechanism, known as quorum sensing (QS). Many bacteria use QS signaling systems to synchronize target gene expression and coordinate biological activities among a local population. N-acylhomoserine lactones (AHLs) are one family of the well-characterized QS signals in Gram-negative bacteria, which regulate a range of important biological functions, including virulence and biofilm formation. Several groups of AHL-degradation enzymes have recently been identified in a range of living organisms, including bacteria and eukaryotes. Expression of these enzymes in AHL-dependent pathogens and transgenic plants efficiently quenches the microbial QS signaling and blocks pathogenic infections. Discovery of these novel quorum quenching enzymes has not only provided a promising means to control bacterial infections, but also presents new challenges to investigate their roles in host organisms and their potential impacts on ecosystems.

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