Identification of Novel Dipeptidyl Peptidase-IV Inhibitory Peptides in Chickpea Protein Hydrolysates

Dipeptidyl peptidase-IV (DPP-IV) is one of the main targetsforblood sugar control. Some food protein-derived peptides are thoughtto have DPP-IV inhibitory (DPP-IVi) activity. In this study, chickpeaprotein hydrolysates (CPHs) obtained through Neutrase hydrolysis for60 min (CPHs-Pro-60) exhibited the highest DPP-IVi activity. DPP-IViactivity after simulated in vitro gastrointestinaldigestion was maintained at >60%. Peptide libraries are establishedafter the identification of peptide sequences. Molecular docking verifiedthat the four screened peptides (AAWPGHPEF, LAFP, IAIPPGIPYW, andPPGIPYW) could bind to the active center of DPP-IV. Notably, IAIPPGIPYWexhibited the most potent DPP-IVi activity (half maximal inhibitoryconcentration (IC50): 12.43 mu M). Both IAIPPGIPYWand PPGIPYW exhibited excellent DPP-IVi activity in Caco-2 cells.These results indicated that chickpea could be used as a source ofnatural hypoglycemic peptides for food and nutritional applications.

Automated summary

This study found that chickpea protein hydrolysates (CPHs) obtained through Neutrase hydrolysis had high DPP-IV inhibitory (DPP-IVi) activity. Four peptides with strong DPP-IVi activity were identified through peptide sequence analysis and molecular docking, among which IAIPPGIPYW showed the strongest activity. Chickpea could be used as a natural source of hypoglycemic peptides.