Journal of Microbiology

Journal Article

Identification of a novel phospholipase D gene and effects of carbon sources on its expression in Bacillus cereus ZY12: Yu Zhao , Yinfeng Xu , Fang Yu , Chunzhi Zhang; J. Microbiol. 2018;56(4):264-271. Published online April 2, 2018; DOI: https://doi.org/10.1007/s12275-018-7529-1

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In the present study, a new strain, Bacillus cereus ZY12, producing phospholipase D (PLD) was identified. The expression of PLD in this strain was found to be induced by its substrate, phosphatidylcholine (PC), and completely silenced by other carbon sources, such as glucose, fructose, and maltose, which are generally used in microbial growth cultures, thus presenting a unique expression pattern different from other PLD-producing microorganisms. This study is the first to report on the ability of B. cereus to produce PLD, and successfully clone its PLD-coding gene and identify its function, extending the knowledge on PLD distribution and evolution in microorganisms.

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Efficient Extracellular Production of Phospholipase D in Escherichia coli via Genetic and Process Engineering Modification
Huan Liu, Yang Yang, Tianyi Wang, Yuchen Ning, Li Deng, Fang Wang
Synthetic Biology and Engineering.2025; 3(2): 10006. CrossRef
Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA
Xiaoyun Yang, Zongqiang Li, Liang Zhao, Zhun She, Zengqiang Gao, Sen-Fang Sui, Yuhui Dong, Yanhua Li
Nature Communications.2022;[Epub] CrossRef
Construction of a Super-Folder Fluorescent Protein-Guided Secretory Expression System for the Production of Phospholipase D in Bacillus subtilis
Haiyang Zhang, Xuehan Li, Qi Liu, Jianan Sun, Francesco Secundo, Xiangzhao Mao
Journal of Agricultural and Food Chemistry.2021; 69(24): 6842. CrossRef
Microbial phospholipase D: Identification, modification and application
Zhenxia Zhang, Ming Chen, Wei Xu, Wenli Zhang, Tao Zhang, Cuie Guang, Wanmeng Mu
Trends in Food Science & Technology.2020; 96: 145. CrossRef

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

NOTE] Bacillus manliponensis sp. nov., a New Member of the Bacillus cereus Group Isolated from Foreshore Tidal Flat Sediment: Min Young Jung , Joong-Su Kim , Woon Kee Paek , Jeongheui Lim , Hansoo Lee , Pyoung Il Kim , Jin Yeul Ma , Wonyong Kim , Young-Hyo Chang; J. Microbiol. 2011;49(6):1027-1032. Published online December 28, 2011; DOI: https://doi.org/10.1007/s12275-011-1049-6

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Abstract

A Gram-positive, endospore-forming, new Bacillus species, strain BL4-6T, was isolated from tidal flat sediment of the Yellow Sea. Strain BL4-6T is a straight rod, with motility by peritrichate flagella. The cell wall contains meso-diaminopimelic acid, and the major respiratory quinone is menaquinone-7. The major fatty acids are iso-C15:0 and summed feature 3 (containing C16:1 ω7c/ iso-C15:0 2OH, and/or iso-C15:0 2OH/C16:1 ω7c). Cells are catalase-positive and oxidase-negative. The G+C content of the genomic DNA is 38.0 mol%. Based on a comparative 16S rRNA gene sequence analysis, the isolate belongs to the genus Bacillus, forms a clade with the Bacillus cereus group, and is closely related to Bacillus mycoides (98.5%), Bacillus cereus (98.5%), Bacillus anthracis (98.4%), Bacillus thuringiensis (98.4%), Bacillus weihenstephanensis (98.1%), and Bacillus pseudomycoides (97.5%). The isolate showed less than 85% similarity of the gyrA gene sequence and below 95% similarity of the rpoB gene sequence to the members of this group. DNA-DNA relatedness between strain BL4-6T and B. cereus group was found to be in a range of 22.8-42.3%, and thus BL4-6T represents a unique species. On the basis of these studies, strain BL4-6T (=KCTC 13319T =JCM 15802T) is proposed to represent the type strain of a novel species, Bacillus manliponensis sp. nov.

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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]

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Abstract: 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.

Editorial

[SPECIAL ISSUE]Two years of COVID-19 pandemic: where are we now?: Jinjong Myoung; J. Microbiol. 2022;60(3):235-237.; DOI: https://doi.org/10.1007/s12275-022-1679-x

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Characterization of Bacillus cereus SH-7 Extracellular Protease: Hak Kyu Yi , Young Jin Chum , Han Bok Kim; J. Microbiol. 1999;37(4):213-217.

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Abstract: 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.

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