Journal of Microbiology

Journal Article

Heterologous expression and enzymatic characterization of γ-glutamyltranspeptidase from Bacillus amyloliquefaciens: Jung-Min Lee , Jaejung Lee , Gyeong-Hwa Nam , Byung-Sam Son , Myoung-Uoon Jang , So-Won Lee , Byung-Serk Hurh , Tae-Jip Kim; J. Microbiol. 2017;55(2):147-152. Published online January 26, 2017; DOI: https://doi.org/10.1007/s12275-017-6638-6

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γ-Glutamyltranspeptidase (GGT) catalyzes the cleavage of γ- glutamyl compounds and the transfer of γ-glutamyl moiety to water or to amino acid/peptide acceptors. GGT can be utilized for the generation of γ-glutamyl peptides or glutamic acid, which are used as food taste enhancers. In the present study, Bacillus amyloliquefaciens SMB469 with high GGT activity was isolated from Doenjang, a traditional fermented soy food of Korea. The gene encoding GGT from B. amyloliquefaciens SMB469 (BaGGT469) was cloned from the isolate, and heterologously expressed in E. coli and B. subtilis. For comparison, three additional GGT genes were cloned from B. subtilis 168, B. licheniformis DSM 13, and B. amyloliquefaciens FZB42. The BaGGT469 protein was composed of 591 amino acids. The final protein comprises two separate polypeptide chains of 45.7 and 19.7 kDa, generated via autocatalytic cleavage. The specific activity of BaGGT469 was determined to be 17.8 U/mg with γ-L-glutamyl-p-nitroanilide as the substrate and diglycine as the acceptor. GGTs from B. amyloliquefaciens showed 1.4- and 1.7-fold higher transpeptidase activities than those from B. subtilis and B. licheniformis, respectively. Especially, recombinant B. subtilis expressing BaGGT469 demonstrated 11- and 23-fold higher GGT activity than recombinant E. coli and the native B. amyloliquefaciens, respectively, did. These results suggest that BaGGT469 can be utilized for the enzymatic production of various γ- glutamyl compounds.

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Gram-positive Rhizobacterium Bacillus amyloliquefaciens FZB42 Colonizes Three Types of Plants in Different Patterns: Ben Fan , Rainer Borriss , Wilfrid Bleiss , Xiaoqin Wu; J. Microbiol. 2012;50(1):38-44. Published online February 27, 2012; DOI: https://doi.org/10.1007/s12275-012-1439-4

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Abstract: The colonization of three types of different plants, Zea mays, Arabidopsis thaliana, and Lemna minor, by GFP-labeled Gram-positive rhizobacterium Bacillus amyloliquefaciens FZB42 was studied in gnotobiotic systems using confocal laser scanning microscopy and electron microscopy. It was demonstrated that FZB42 was able to colonize all the plants. On one hand, similar to some Gram-negative rhizobacteria like Pseudomonas, FZB42 favored the areas such as the concavities in root surfaces and the junctions where lateral roots occurred from the primary roots; on the other hand, we clearly demonstrated that root hairs were a popular habitat to the Gram-positive rhizobacterium. FZB42 exhibited a specific colonization pattern on each of the three types of plants. On Arabidopsis, tips of primary roots were favored by FZB42 but not so on maize. On Lemna, FZB42 accumulated preferably along the grooves between epidermal cells of roots and in the concave spaces on ventral sides of fronds. The results suggested L. minor to be a promising tool for investigations on plant-microbial interaction due to a series of advantages it has. Colonization of maize and Arabidopsis roots by FZB42 was also studied in the soil system. Comparatively, higher amount of FZB42 inoculum (~108 CFU/ml) was required for detectable root colonization in the soil system, where the preference of FZB42 cells to root hairs were also observed.

Multicatalytic Alkaline Serine Protease from the Psychrotrophic Bacillus amyloliquefaciens S94: Eui-Sun Son , Jong-Il Kim; J. Microbiol. 2003;41(1):58-62.

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Abstract: 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.

Calcite Production by Bacillus amyloliquefaciens CMB01: Young Nam Lee; J. Microbiol. 2003;41(4):345-348.

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Abstract: The bio-mediated production of calcite crystals by calcinogenic bacteria has great applicable value for the restoration of deteriorated calcareous monuments, because of its high purity and coherency. An investigation of the conditions for calcite production by an alkalophilic Bacillus amyloliquefaciens CMB01 strain was made. Optimal calcite precipitation occurred when the bacterium was cultured at pH 8.0 and 30℃, and in B4 medium that consisted of 0.4% yeast extract, 0.5% glucose, and 1.5% calcium acetate. Calcium ion of the bacterially induced calcite was analyzed by an inductively coupled plasma (ICP) spectrophotometer. Optical and scanning electron microscopy (SEM) of the calcite revealed a typical rombohedral polycrystalline structure.

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