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Peptides in Common Bean Protein Hydrolysates Inhibit Molecular Target Enzymes in type‐2 Diabetes

The objective was to optimize the enzymatic production of peptides with potential to inhibit carbohydrate degradation related enzymes (α‐amylase and α‐glucosidase). Black bean protein isolate was hydrolyzed using either flavourzyme, papain, alcalase, thermolysin, tripsin, chymotrypsin, proteinase k or pepsin at three ratios (1:20, 1:30, 1:50 E/S) and three times of hydrolysis (2, 3, 4 h). Percent inhibition of α‐amylase or α‐glucosidase were used as optimization parameters. Considering the response surface analysis output, the best protease was alcalase; for all tested proteases, 2 h of hydrolysis and 1:20 E/S showed the optimal inhibition (p= 0.001) with α‐amylase and α‐glucosidase of 66.2± 2.2%/mg of hydrolysate and 53.5 ± 2.9% /mg of hydrolysate, respectively. The in silico study revealed 68 peptides ranging from 2 to 21 amino acids derived from phaseolin amino acid sequence with molecular masses ranging from 280.3 to 2329.4 Da. Bioactivity from Biopep database showed potential bioactivities related with angiotensin converting enzyme inhibition (37.6%), dipeptidyl peptidase‐IV inhibition (21.2%), and antioxidative properties (15.6%). Results indicated that peptides from black bean protein hydrolysates have potential to inhibit enzymes used as molecular targets in the management of type‐2 diabetes.