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

The kokumi sensation of protein hydrolysates could be enhanced by gamma-glutamylation through forming a series of gamma- glutamyl di-and tri-peptides. In this study, porcine hemoglobin hydrolysate was gamma-glutamylated using enzymes from Bacillus amyloliquefaciens (Ba) or Bacillus licheniformis (Bl), which are sold as glutaminases but identified as gamma-glutamyltransferases (GGTs). To yield more gamma-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 gamma-glutamyl dipeptides, while BlGGT was more capable to generate gamma-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.

Automated summary

The kokumi sensation of protein hydrolysates can be enhanced by gamma-glutamylation. Porcine hemoglobin hydrolysate was gamma-glutamylated using enzymes from Bacillus amyloliquefaciens or Bacillus licheniformis. Both enzymes showed high transpeptidase activity, with different temperature preferences. Adding glutamine was more efficient in producing target peptides.