Enhancement of glutaryl‐7‐aminocephalosporanic acid acylase activity of γ‐glutamyltranspeptidase of <i>Bacillus subtilis</i>

Suzuki, Hideyuki; Yamada, Chiaki; Kijima, Kyoko; Ishihara, Sayaka; Wada, Keita; Fukuyama, Keiichi; Kumagai, Hidehiko

doi:10.1002/biot.201000015

Cited by 13 publications

(10 citation statements)

References 22 publications

(26 reference statements)

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“…Escherichia coli K-12 strain SH641 (F − ∆ggt-2 rpsL recA56 srl300 ::Tn10 ) was transformed with this plasmid pCY167 and strain CY168 was obtained (Suzuki et al, 2010).…”

Section: Bacterial Strain Used In This Studymentioning

confidence: 99%

Increase of “Umami” and “Kokumi” Compounds in Miso, Fermented Soybeans, by the Addition of Bacterial γ-Glutamyltranspeptidase

Suzuki

2013

Int. J. Food Stud.

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γ-Glutamyltranspeptidase (GGT) hydrolyzes γ-glutamyl compounds and transfers their γ-glutamyl moieties to amino acids and peptides. We previously showed that the "umami" taste of soy sauce could be improved by the addition of salt-tolerant Bacillus subtilis GGT to the fermentation mixture, "moromi". Although miso fermentation is a semi-solid fermentation, unlike soy sauce fermentation, this was also the case. When 15 units of purified B. subtilis GGT were added to 418 g miso "moromi" (fermentation mixture), the glutamate concentration in "moromi" became 20 mM higher and the "umami" taste became stronger than without the addition of GGT after 2 to 6 months of fermentation. In addition, γ-Glu-Val and γ-Glu-Val-Gly, which are known as "kokumi" peptides, were identified in "tamari", and the concentrations of these γ-glutamyl peptides in "tamari" fermented by the addition of GGT were significantly higher than those of "moromi" without the addition of GGT. These results indicate that B. subtilis GGT is able to improve the taste of miso.

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“…Escherichia coli K-12 strain SH641 (F − ∆ggt-2 rpsL recA56 srl300 ::Tn10 ) was transformed with this plasmid pCY167 and strain CY168 was obtained (Suzuki et al, 2010).…”

Section: Bacterial Strain Used In This Studymentioning

confidence: 99%

Increase of “Umami” and “Kokumi” Compounds in Miso, Fermented Soybeans, by the Addition of Bacterial γ-Glutamyltranspeptidase

Suzuki

2013

Int. J. Food Stud.

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“…Since we found B. subtilis GGT has inherent glutaryl-7-ACA acylase activity and we also determined its three-dimensional structure 38 , mutations were introduced into B. subtilis GGT and eventually the enzyme catalytic efficiency k cat /K m became higher than class IV cephalosporin acylase from Pseudomonas sp. V22 39 . Our mutation work on GGTs thus made the enzymes exert the acylase activity capable of making cephalosporin antibiotic.…”

Section: Mutagenic Conversion Of Ggt To Glutaryl-7-aminocephalosporanmentioning

confidence: 99%

Bacterial γ-glutamyltranspeptidase: Food and medicinal applications

Suzuki¹

2019

ScienceAsia

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γ-Glutamyltranspeptidase (GGT) catalyzes the hydrolysis of γ-glutamyl compounds and the transfer of their γ-glutamyl moiety to another amino acids or peptides. We have proposed several applications of this enzyme, especially in food and medicine, for the wellness of humans. These applications depend on the fact that the pH optima of the hydrolysis and transpeptidase reactions are distinctly different in E. coli GGT. The applications of bacterial GGTs are introduced in this review.

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“…Plasmid pCY167 (ColE1 ori bla + lacI q rrnBT1 T5p-ggt B.subtilis ) is a derivative of pQE-80L harboring a signal peptide, large and small subunits of B. subtilis GGT following the initiation codon, but it does not have a His-tag; that is, the nucleotide sequence within the open reading frame is exactly the same as the wild-type B. subtilis ggt gene. Escherichia coli K-12 strain SH641 (F − ∆ggt-2 rpsL recA56 srl300 ::Tn10 ) was transformed with this plasmid pCY167 and strain CY168 was obtained (Suzuki et al, 2010).…”

Section: Bacterial Strain Used In This Studymentioning

confidence: 99%

Increase of “Umami” and “Kokumi” Compounds in Miso, Fermented Soybeans, by the Addition of Bacterial γ-Glutamyltranspeptidase

Ho¹,

Suzuki

2013

Int. J. Food Stud.

Self Cite

View full text Add to dashboard Cite

γ-Glutamyltranspeptidase (GGT) hydrolyzes γ-glutamyl compounds and transfers their γ-glutamyl moieties to amino acids and peptides. We previously showed that the “umami” taste of soy sauce could be improved by the addition of salt-tolerant Bacillus subtilis GGT to the fermentation mixture, “moromi”. Although miso fermentation is a semi-solid fermentation, unlike soy sauce fermentation, this was also the case. When 15 units of purified B. subtilis GGT were added to 418 g miso “moromi” (fermentation mixture), the glutamate concentration in “moromi” became 20 mM higher and the “umami” taste became stronger than without the addition of GGT after 2 to 6 months of fermentation. In addition, γ-Glu-Val and γ-Glu-Val-Gly, which are known as “kokumi” peptides, were identified in “tamari”, and the concentrations of these γ-glutamyl peptides in “tamari" fermented by the addition of GGT were significantly higher than those of “moromi” without the addition of GGT. These results indicate that B. subtilis GGT is able to improve the taste of miso.

show abstract

Enhancement of glutaryl‐7‐aminocephalosporanic acid acylase activity of γ‐glutamyltranspeptidase of Bacillus subtilis

Cited by 13 publications

References 22 publications

Increase of “Umami” and “Kokumi” Compounds in Miso, Fermented Soybeans, by the Addition of Bacterial γ-Glutamyltranspeptidase

Increase of “Umami” and “Kokumi” Compounds in Miso, Fermented Soybeans, by the Addition of Bacterial γ-Glutamyltranspeptidase

Bacterial γ-glutamyltranspeptidase: Food and medicinal applications

Increase of “Umami” and “Kokumi” Compounds in Miso, Fermented Soybeans, by the Addition of Bacterial γ-Glutamyltranspeptidase

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