In this study, the peptides of soy protein obtained by enzymatic digestion with proteases were analyzed for their antidiabetic, antihypertensive, and antioxidant activities. Peptides prepared with alkaline proteinase (AP) exhibited the highest α-glucosidase inhibitory activity compared with those from papain and trypsin digestion. AP hydrolysates also exhibited dipeptidyl peptidase IV (DPP-IV) inhibitory, angiotensin-converting enzyme (ACE) inhibitory, and antioxidant activities. Gastrointestinal digestion of peptides enhanced α-glucosidase, DPP-IV, and ACE inhibitory activities compared with AP hydrolysates. AP peptides showing highest α-glucosidase inhibitory activity were purified by anion-exchange and size-exclusion chromatography， and identified using tandem MS. We found three novel α-glucosidase inhibitory peptides with sequences LLPLPVLK, SWLRL, and WLRL with IC50 of 237.43 ± 0.52, 182.05 ± 0.74, and 162.29 ± 0.74 μmol/L, respectively. Therefore, peptides hydrolyzed from soy protein are promising natural ingredients for nutraceutical applications assisting in the management of diabetes.
Keywords: ACE inhibitory activity; antidiabetic activity; antioxidant activity; peptide; soy protein; α‐glucosidase inhibitory activity.