10148-81-9Relevant articles and documents
Enzymatic Synthesis of γ-Glutamylvaline to Improve the Bitter Taste of Valine
Suzuki, Hideyuki,Kato, Kenji,Kumagai, Hidehiko
, p. 577 - 580 (2004)
The taste of several bitter amino acids is reduced, sourness produced, and preference increased by γ-glutamylization. An enzymatic method for synthesizing γ-Glu-Val involving bacterial γ-glutamyltranspeptidase (GGT) was developed. The optimum reaction conditions for the synthesis of γ-Glu-Val were 20 mM Gln, 300 mM Val, and 0.04 U/ml GGT, pH 10. After 3-hr incubation at 37 °C, 17.6 mM γ-Glu-Val was obtained, with the yield being 88%. γ-Glu-Val was purified on a Dowex 1 × 8 column and then identified by NMR.
PH-Dependent hydrolase, glutaminase, transpeptidase and autotranspeptidase activities of Bacillus subtilis γ-glutamyltransferase
Morelli, Carlo F.,Calvio, Cinzia,Biagiotti, Marco,Speranza, Giovanna
, p. 232 - 245 (2014/01/23)
γ-Glutamyltransferases (γ-GTs) are heterodimeric enzymes that catalyze the transfer of a γ-glutamyl group from a donor species to an acceptor molecule in a transpeptidation reaction through the formation of an intermediate γ-glutamyl enzyme. In our search for a γ-GT from a generally recognized as safe microorganism suitable for the production of γ-glutamyl derivatives with flavor-enhancing properties intended for human use, we cloned and overexpressed the γ-GT from Bacillus subtilis. In this study, we report the behavior of B. subtilis γ-GT in reactions involving glutamine as the donor compound and various acceptor amino acids. The common thread emerging from our results is a strong dependence of the hydrolase, transpeptidase and autotranspeptidase activities of B. subtilis γ-GT on pH, also in relation to the pKa of the acceptor amino acids. Glutamine, commonly referred to as a poor acceptor molecule, undergoes rapid autotranspeptidation at elevated pH, affording oligomeric species, in which up to four γ-glutamyl moieties are linked to a single glutamine. Moreover, we found that d-glutamine is also recognized both as a donor and as an acceptor substrate. Our results prove that the B. subtilis γ-GT-catalyzed transpeptidation reaction is feasible, and the observed activities of γ-GT from B. subtilis could be interpreted in relation to the known ability of the enzyme to process the polymeric material γ-polyglutamic acid.
Formation of γ-Glutamyl Peptides by Glutaminase of Aspergillus oryzae
Tomita, Kenji,Yano, Toshihiro,Kitagata, Tatsuichiro,Kumagai, Hidehiko,Tochikura, Tatsurokuro
, p. 1995 - 1996 (2007/10/02)
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