Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase

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

Standard

Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase. / Li, Qian; Zhang, Longteng; Lametsch, René.

In: Journal of Agricultural and Food Chemistry, Vol. 70, No. 50, 2022, p. 15894–15902.

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

Harvard

Li, Q, Zhang, L & Lametsch, R 2022, 'Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase', Journal of Agricultural and Food Chemistry, vol. 70, no. 50, pp. 15894–15902. https://doi.org/10.1021/acs.jafc.2c07045

APA

Li, Q., Zhang, L., & Lametsch, R. (2022). Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase. Journal of Agricultural and Food Chemistry, 70(50), 15894–15902. https://doi.org/10.1021/acs.jafc.2c07045

Vancouver

Li Q, Zhang L, Lametsch R. Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase. Journal of Agricultural and Food Chemistry. 2022;70(50):15894–15902. https://doi.org/10.1021/acs.jafc.2c07045

Author

Li, Qian ; Zhang, Longteng ; Lametsch, René. / Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase. In: Journal of Agricultural and Food Chemistry. 2022 ; Vol. 70, No. 50. pp. 15894–15902.

Bibtex

@article{a20a2c781d9340389514dcf1bd3af1aa,
title = "Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase",
abstract = "The kokumi sensation of protein hydrolysates could be enhanced by γ-glutamylation through forming a series of γ-glutamyl di- and tri-peptides. In this study, porcine hemoglobin hydrolysate was γ-glutamylated using enzymes from Bacillus amyloliquefaciens (Ba) or Bacillus licheniformis (Bl), which are sold as glutaminases but identified as γ-glutamyltransferases (GGTs). To yield more γ-glutamyl peptides, reaction conditions were optimized in terms of GGT source (BaGGT and BlGGT), substrate concentration (10, 20, and 40%), reaction time (3, 6, 12, and 24 h), and glutamine supplementation (20, 40, and 80 mM). Results showed that both the GGTs had the highest transpeptidase activity at similar pH values but different temperatures. In addition, BaGGT had stronger catalytic ability to form γ-glutamyl dipeptides, while BlGGT was more capable to generate γ-Glu-Val-Gly. Adding glutamine was more efficient to obtain more target peptides than adjusting the hydrolysate concentration and reaction time. This study contributes to the valorization of animal side streams. ",
keywords = "Bacillus licheniformis, hemoglobin hydrolysate, γ-glutamyl peptides, γ-glutamyltransferase",
author = "Qian Li and Longteng Zhang and Ren{\'e} Lametsch",
note = "Publisher Copyright: {\textcopyright} 2022 American Chemical Society.",
year = "2022",
doi = "10.1021/acs.jafc.2c07045",
language = "English",
volume = "70",
pages = "15894–15902",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "50",

}

RIS

TY - JOUR

T1 - Increase of Kokumi γ-Glutamyl Peptides in Porcine Hemoglobin Hydrolysate Using Bacterial γ-Glutamyltransferase

AU - Li, Qian

AU - Zhang, Longteng

AU - Lametsch, René

N1 - Publisher Copyright: © 2022 American Chemical Society.

PY - 2022

Y1 - 2022

N2 - The kokumi sensation of protein hydrolysates could be enhanced by γ-glutamylation through forming a series of γ-glutamyl di- and tri-peptides. In this study, porcine hemoglobin hydrolysate was γ-glutamylated using enzymes from Bacillus amyloliquefaciens (Ba) or Bacillus licheniformis (Bl), which are sold as glutaminases but identified as γ-glutamyltransferases (GGTs). To yield more γ-glutamyl peptides, reaction conditions were optimized in terms of GGT source (BaGGT and BlGGT), substrate concentration (10, 20, and 40%), reaction time (3, 6, 12, and 24 h), and glutamine supplementation (20, 40, and 80 mM). Results showed that both the GGTs had the highest transpeptidase activity at similar pH values but different temperatures. In addition, BaGGT had stronger catalytic ability to form γ-glutamyl dipeptides, while BlGGT was more capable to generate γ-Glu-Val-Gly. Adding glutamine was more efficient to obtain more target peptides than adjusting the hydrolysate concentration and reaction time. This study contributes to the valorization of animal side streams.

AB - The kokumi sensation of protein hydrolysates could be enhanced by γ-glutamylation through forming a series of γ-glutamyl di- and tri-peptides. In this study, porcine hemoglobin hydrolysate was γ-glutamylated using enzymes from Bacillus amyloliquefaciens (Ba) or Bacillus licheniformis (Bl), which are sold as glutaminases but identified as γ-glutamyltransferases (GGTs). To yield more γ-glutamyl peptides, reaction conditions were optimized in terms of GGT source (BaGGT and BlGGT), substrate concentration (10, 20, and 40%), reaction time (3, 6, 12, and 24 h), and glutamine supplementation (20, 40, and 80 mM). Results showed that both the GGTs had the highest transpeptidase activity at similar pH values but different temperatures. In addition, BaGGT had stronger catalytic ability to form γ-glutamyl dipeptides, while BlGGT was more capable to generate γ-Glu-Val-Gly. Adding glutamine was more efficient to obtain more target peptides than adjusting the hydrolysate concentration and reaction time. This study contributes to the valorization of animal side streams.

KW - Bacillus licheniformis

KW - hemoglobin hydrolysate

KW - γ-glutamyl peptides

KW - γ-glutamyltransferase

U2 - 10.1021/acs.jafc.2c07045

DO - 10.1021/acs.jafc.2c07045

M3 - Journal article

C2 - 36473160

AN - SCOPUS:85143712127

VL - 70

SP - 15894

EP - 15902

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 50

ER -

ID: 329708581