- Whole genome analysis of Aspergillus sojae SMF 134 supports its merits as a starter for soybean fermentation
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Kang Uk Kim , Kyung Min Kim , Yong-Ho Choi , Byung-Serk Hurh , Inhyung Lee
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J. Microbiol. 2019;57(10):874-883. Published online June 27, 2019
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DOI: https://doi.org/10.1007/s12275-019-9152-1
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 Abstract
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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.
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Citations
Citations to this article as recorded by  - Population Genomics of Aspergillus sojae is Shaped by the Food Environment
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- Heterologous expression and enzymatic characterization of γ-glutamyltranspeptidase from Bacillus amyloliquefaciens
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Jung-Min Lee , Jaejung Lee , Gyeong-Hwa Nam , Byung-Sam Son , Myoung-Uoon Jang , So-Won Lee , Byung-Serk Hurh , Tae-Jip Kim
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J. Microbiol. 2017;55(2):147-152. Published online January 26, 2017
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DOI: https://doi.org/10.1007/s12275-017-6638-6
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1,071
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Abstract
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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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