Comparative analysis of substrate affinity and catalytic efficiency of γ-glutamyltransferase from bovine milk and Bacillus amyloliquefaciens

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Comparative analysis of substrate affinity and catalytic efficiency of γ-glutamyltransferase from bovine milk and Bacillus amyloliquefaciens. / Cao, Lichuang; Li, Qian; Lametsch, René.

In: Food Chemistry, Vol. 405, 134930, 2023.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Cao, L, Li, Q & Lametsch, R 2023, 'Comparative analysis of substrate affinity and catalytic efficiency of γ-glutamyltransferase from bovine milk and Bacillus amyloliquefaciens', Food Chemistry, vol. 405, 134930. https://doi.org/10.1016/j.foodchem.2022.134930

APA

Cao, L., Li, Q., & Lametsch, R. (2023). Comparative analysis of substrate affinity and catalytic efficiency of γ-glutamyltransferase from bovine milk and Bacillus amyloliquefaciens. Food Chemistry, 405, [134930]. https://doi.org/10.1016/j.foodchem.2022.134930

Vancouver

Cao L, Li Q, Lametsch R. Comparative analysis of substrate affinity and catalytic efficiency of γ-glutamyltransferase from bovine milk and Bacillus amyloliquefaciens. Food Chemistry. 2023;405. 134930. https://doi.org/10.1016/j.foodchem.2022.134930

Author

Cao, Lichuang ; Li, Qian ; Lametsch, René. / Comparative analysis of substrate affinity and catalytic efficiency of γ-glutamyltransferase from bovine milk and Bacillus amyloliquefaciens. In: Food Chemistry. 2023 ; Vol. 405.

Bibtex

@article{d8122b247de54b7098e585d3310be819,
title = "Comparative analysis of substrate affinity and catalytic efficiency of γ-glutamyltransferase from bovine milk and Bacillus amyloliquefaciens",
abstract = "This study aimed to characterize the substrate affinity and catalytic efficiency of bovine milk γ-glutamyltransferase (BoGGT) towards different donors and acceptors by comparing it with a reference (Bacillus amyloliquefaciens, BaGGT). Quantitation of γ-glutamyl peptides and free amino acids was conducted in combination with enzymatic kinetic. Kokumi peptides were generated from whey protein hydrolysates through transpeptidation catalyzed by both GGTs. BaGGT has a higher transpeptidase activity than BoGGT when γ-glutamyl-p-nitroanilide (γ-GpNA) or glutamine acts as a donor. Glutamine is a better γ-glutamyl donor than γ-GpNA for both GGTs. Furthermore, membrane-free BoGGT has a more efficient activity and higher substrate affinity than the native BoGGT. BoGGT has the highest affinity with Val-Gly and can produce γ-Glu-Val-Gly, a substance with a strong kokumi intensity and the lowest taste threshold. This study reveals that the catalytic ability of GGT is highly dependent on the acceptor, and membrane interactions restrict the transpeptidase activity of BoGGT.",
keywords = "Enzymatic kinetic, Kokumi peptides, LC-MS/MS quantification, Skim milk membrane, γ-Glutamyltransferase",
author = "Lichuang Cao and Qian Li and Ren{\'e} Lametsch",
note = "Publisher Copyright: {\textcopyright} 2022 Elsevier Ltd",
year = "2023",
doi = "10.1016/j.foodchem.2022.134930",
language = "English",
volume = "405",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Comparative analysis of substrate affinity and catalytic efficiency of γ-glutamyltransferase from bovine milk and Bacillus amyloliquefaciens

AU - Cao, Lichuang

AU - Li, Qian

AU - Lametsch, René

N1 - Publisher Copyright: © 2022 Elsevier Ltd

PY - 2023

Y1 - 2023

N2 - This study aimed to characterize the substrate affinity and catalytic efficiency of bovine milk γ-glutamyltransferase (BoGGT) towards different donors and acceptors by comparing it with a reference (Bacillus amyloliquefaciens, BaGGT). Quantitation of γ-glutamyl peptides and free amino acids was conducted in combination with enzymatic kinetic. Kokumi peptides were generated from whey protein hydrolysates through transpeptidation catalyzed by both GGTs. BaGGT has a higher transpeptidase activity than BoGGT when γ-glutamyl-p-nitroanilide (γ-GpNA) or glutamine acts as a donor. Glutamine is a better γ-glutamyl donor than γ-GpNA for both GGTs. Furthermore, membrane-free BoGGT has a more efficient activity and higher substrate affinity than the native BoGGT. BoGGT has the highest affinity with Val-Gly and can produce γ-Glu-Val-Gly, a substance with a strong kokumi intensity and the lowest taste threshold. This study reveals that the catalytic ability of GGT is highly dependent on the acceptor, and membrane interactions restrict the transpeptidase activity of BoGGT.

AB - This study aimed to characterize the substrate affinity and catalytic efficiency of bovine milk γ-glutamyltransferase (BoGGT) towards different donors and acceptors by comparing it with a reference (Bacillus amyloliquefaciens, BaGGT). Quantitation of γ-glutamyl peptides and free amino acids was conducted in combination with enzymatic kinetic. Kokumi peptides were generated from whey protein hydrolysates through transpeptidation catalyzed by both GGTs. BaGGT has a higher transpeptidase activity than BoGGT when γ-glutamyl-p-nitroanilide (γ-GpNA) or glutamine acts as a donor. Glutamine is a better γ-glutamyl donor than γ-GpNA for both GGTs. Furthermore, membrane-free BoGGT has a more efficient activity and higher substrate affinity than the native BoGGT. BoGGT has the highest affinity with Val-Gly and can produce γ-Glu-Val-Gly, a substance with a strong kokumi intensity and the lowest taste threshold. This study reveals that the catalytic ability of GGT is highly dependent on the acceptor, and membrane interactions restrict the transpeptidase activity of BoGGT.

KW - Enzymatic kinetic

KW - Kokumi peptides

KW - LC-MS/MS quantification

KW - Skim milk membrane

KW - γ-Glutamyltransferase

U2 - 10.1016/j.foodchem.2022.134930

DO - 10.1016/j.foodchem.2022.134930

M3 - Journal article

C2 - 36410217

AN - SCOPUS:85142136676

VL - 405

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

M1 - 134930

ER -

ID: 332699201