Abstract: The nutritional composition and the anti-exopeptidase digestion structures of pea oligopeptides were investigated. The results showed that the pea oligopeptide had a protein content of 86.27% and an oligopeptide content of 81.82%. The relative molecular weight was mainly in the range of 140-1 000 Da, accounting for 83.61% of the total proportion. The essential amino acid content was 27.61%, accounting for 33.37% of the total. Glutamic acid content was 16.61%, ranking the first of all amino acids, which was the precursor of pyroglutamic acid. Structural identification results showed that pea oligopeptides contained three dipeptides, pyroglutamyl-lysine (pEK), pyroglutamyl-glutamate (pEE), and pyroglutamyl-arginine (pER), the contents of which were 201.85, 75.30 and 110.84 mg/100 g, respectively. After digestion by leucine aminopeptidase and carboxypeptidase A, the contents of three peptides were all increased, indicating that the three peptides were resistant to exopeptidase digestion, which may express functional activity in the body. These three peptides were all first found in pea oligopeptides.
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