LAUSR

In this study, flavourzyme, papain, neutrase, and alcalase, as well as gastrointestinal digestion simulated with pepsin and pancreatin, were used to hydrolyze oat protein, and the dipeptidyl peptidase-IV (DPP-IV) inhibitory activities of the oat protein hydrolysates were investigated. The results indicated that the oat protein hydrolysate by neutrase showed the most potent DPP-IV inhibitory property with an IC50 value of 2.55 ± 0.38 mg/mL. Using UPLC-MS/MS, ten new DPP-IV inhibitory peptides were identified from the oat protein hydrolysate by neutrase. Among these peptides, IPQHY, VPQHY, VAVVPF, and VPLGGF exhibited the strongest DPP-IV inhibitory activity with IC50 values below 50 μM, and all of them acted as mixed-type inhibitors. Molecular docking indicated that the above four oat-derived peptides were predicted to form hydrogen bonds, attractive charge, and hydrophobic interactions with the residues of the active site of DPP-IV. Therefore, our results suggest that oat is an excellent protein source for food-derived DPP-IV inhibitory peptides and it has the prospect of becoming a dietary supplement for T2DM.