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γ ‐Glu‐Met synthesised using a bacterial glutaminase as a potential inhibitor of dipeptidyl peptidase IV
Author(s) -
Yang Juan,
SunWaterhouse Dongxiao,
Cui Chun,
Dong Keming,
Zhao Mouming
Publication year - 2018
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13692
Subject(s) - glutaminase , chemistry , enzyme , residue (chemistry) , biochemistry , stereochemistry , amino acid , glutamine
Summary This study describes γ ‐glutamyl dipeptides as competitive inhibitors of dipeptidyl peptidase‐IV (DPP‐IV), and the feasible synthesis of γ ‐Glu‐Met through transpeptidation catalysed by a commercial glutaminase of Bacillus amyloliquefaciens . γ ‐Glu‐Met, γ ‐Glu‐Leu, γ ‐Glu‐Phe, γ ‐Glu‐Trp or γ ‐Glu‐Tyr exhibited a competitive inhibitory effect on DPP‐IV. The yield of γ ‐Glu‐Met was 26.16% under optimised conditions: 200 m m Gln, 20 m m Met, 0.1 U mL −1 enzyme, pH 9.0, 37 °C and reaction time 3 h. For the first time, the side products containing characteristic sequences, that is poly‐ γ ‐glutamyl short chains with a terminal Met residue ( γ ‐Glu‐ γ ‐Glu‐Met and γ ‐Glu‐ γ ‐Glu‐ γ ‐Glu‐Met) were identified. The superiority of the commercial glutaminase in the synthesis of DPP‐IV‐inhibitory peptides can enable the application of this novel process for manufacturing γ ‐glutamyl‐peptides as potential functional ingredients in the type 2 diabetic diet.