LAUSR

Corn gluten hydrolysate (CGH) was prepared by food-grade bacterial proteases; alcalase and neutral protease. Digestion of CGH with carboxypeptidase A and leucine aminopeptidase extensively changed elution patterns of peptides from reversed phase high performance liquid chromatography-mass spectrometry (LC-MS), while digestion with pepsin and trypsin hardly affect elution patterns. Twenty-five major peptides in CGH were identified. After digestion with exopeptidases, only prolyl di-peptides and pyroglutamyl di- and tri-peptides remained, whereas the other 17 peptides completely disappeared. On the other hand, all 25 peptides remained after digestion with pepsin and trypsin. These facts suggest that majority of short chain peptides in food protein hydrolysates are degraded by exopeptidases during digestion and absorption processes. Thus, susceptibility to exopeptidases should be considered for prediction of bioactive peptide upon ingestion, which has not been considered in the most of previous studies on food-derived bioactive peptide.