Identification and Activity Characterization of gamma-Glutamyltransferase from Bovine Milk

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Identification and Activity Characterization of gamma-Glutamyltransferase from Bovine Milk. / Cao, Lichuang; Li, Qian; Lametsch, Rene.

In: Journal of Agricultural and Food Chemistry, Vol. 69, No. 50, 2021, p. 15325-15333.

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

Harvard

Cao, L, Li, Q & Lametsch, R 2021, 'Identification and Activity Characterization of gamma-Glutamyltransferase from Bovine Milk', Journal of Agricultural and Food Chemistry, vol. 69, no. 50, pp. 15325-15333. https://doi.org/10.1021/acs.jafc.1c06139

APA

Cao, L., Li, Q., & Lametsch, R. (2021). Identification and Activity Characterization of gamma-Glutamyltransferase from Bovine Milk. Journal of Agricultural and Food Chemistry, 69(50), 15325-15333. https://doi.org/10.1021/acs.jafc.1c06139

Vancouver

Cao L, Li Q, Lametsch R. Identification and Activity Characterization of gamma-Glutamyltransferase from Bovine Milk. Journal of Agricultural and Food Chemistry. 2021;69(50):15325-15333. https://doi.org/10.1021/acs.jafc.1c06139

Author

Cao, Lichuang ; Li, Qian ; Lametsch, Rene. / Identification and Activity Characterization of gamma-Glutamyltransferase from Bovine Milk. In: Journal of Agricultural and Food Chemistry. 2021 ; Vol. 69, No. 50. pp. 15325-15333.

Bibtex

@article{e0931ffbc17e4c4a8ff0b8ab7327ea2f,
title = "Identification and Activity Characterization of gamma-Glutamyltransferase from Bovine Milk",
abstract = "It is well known that bovine milk contains gamma-glutamyltransferase (GGT) activity. To verify the identity of the GGT and further to characterize the generation of gamma-glutamyl peptides, identification of GGT from bovine milk and quantification of kokumi peptides and free amino acids were performed. GGT was purified from skim milk and identified as the bovine protein (G3N2D8), and it reveals that it is composed of two subunits. Sequence alignment with human GGT and molecular mass determination showed that the bovine GGT was glycosylated and contained an N-terminal transmembrane part. Further activity characterization was performed in comparison with GGT from Bacillus amyloliquefaciens in terms of the ability to generate gamma-glutamyl peptides from casein hydrolysates. During the transpeptidation reaction catalyzed by both GGT, gamma-glutamyl peptides significantly (P < 0.05) increased after gamma-glutamylation; addition of glutamine contributed to the generation of gamma-glutamyl peptides, suggesting that glutamine could act as a gamma-glutamyl donor. This study reveals that the GGT of skim milk membranes is a glycosylated membrane protein that can generate gamma-glutamyl peptides.",
keywords = "skim milk membranes, gamma-Glutamyltransferase, kokumi peptides, free amino acids",
author = "Lichuang Cao and Qian Li and Rene Lametsch",
year = "2021",
doi = "10.1021/acs.jafc.1c06139",
language = "English",
volume = "69",
pages = "15325--15333",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "50",

}

RIS

TY - JOUR

T1 - Identification and Activity Characterization of gamma-Glutamyltransferase from Bovine Milk

AU - Cao, Lichuang

AU - Li, Qian

AU - Lametsch, Rene

PY - 2021

Y1 - 2021

N2 - It is well known that bovine milk contains gamma-glutamyltransferase (GGT) activity. To verify the identity of the GGT and further to characterize the generation of gamma-glutamyl peptides, identification of GGT from bovine milk and quantification of kokumi peptides and free amino acids were performed. GGT was purified from skim milk and identified as the bovine protein (G3N2D8), and it reveals that it is composed of two subunits. Sequence alignment with human GGT and molecular mass determination showed that the bovine GGT was glycosylated and contained an N-terminal transmembrane part. Further activity characterization was performed in comparison with GGT from Bacillus amyloliquefaciens in terms of the ability to generate gamma-glutamyl peptides from casein hydrolysates. During the transpeptidation reaction catalyzed by both GGT, gamma-glutamyl peptides significantly (P < 0.05) increased after gamma-glutamylation; addition of glutamine contributed to the generation of gamma-glutamyl peptides, suggesting that glutamine could act as a gamma-glutamyl donor. This study reveals that the GGT of skim milk membranes is a glycosylated membrane protein that can generate gamma-glutamyl peptides.

AB - It is well known that bovine milk contains gamma-glutamyltransferase (GGT) activity. To verify the identity of the GGT and further to characterize the generation of gamma-glutamyl peptides, identification of GGT from bovine milk and quantification of kokumi peptides and free amino acids were performed. GGT was purified from skim milk and identified as the bovine protein (G3N2D8), and it reveals that it is composed of two subunits. Sequence alignment with human GGT and molecular mass determination showed that the bovine GGT was glycosylated and contained an N-terminal transmembrane part. Further activity characterization was performed in comparison with GGT from Bacillus amyloliquefaciens in terms of the ability to generate gamma-glutamyl peptides from casein hydrolysates. During the transpeptidation reaction catalyzed by both GGT, gamma-glutamyl peptides significantly (P < 0.05) increased after gamma-glutamylation; addition of glutamine contributed to the generation of gamma-glutamyl peptides, suggesting that glutamine could act as a gamma-glutamyl donor. This study reveals that the GGT of skim milk membranes is a glycosylated membrane protein that can generate gamma-glutamyl peptides.

KW - skim milk membranes

KW - gamma-Glutamyltransferase

KW - kokumi peptides

KW - free amino acids

U2 - 10.1021/acs.jafc.1c06139

DO - 10.1021/acs.jafc.1c06139

M3 - Journal article

C2 - 34905359

VL - 69

SP - 15325

EP - 15333

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 50

ER -

ID: 288271568