Purification, identification and molecular mechanism of dipeptidyl peptidase IV inhibitory peptides from discarded shrimp (Penaeus vannamei) head.

DPP-IV plays a key role for regulation of glucose metabolism in the body. The object of this study was to obtain DPP-IV inhibitors from discarded but protein-rich Penaeus vannamei (P. vannamei) head, and to explore the potential mechanism between DPP-IV and its inhibitors. P. vannamei head protein was hydrolyzed by five food grade proteases, respectively. The animal protease hydrolysate showed the highest inhibitory active. Then the hydrolysate was sequentially separated by ultrafiltration, gel filtration chromatography and reversed phase high-performance liquid chromatography (RP-HPLC), the peptides sequences were identified by LC-MS/MS and four potential peptides YPGE, VPW, HPLY, YATP showed superior DPP-IV inhibitory activity. Meanwhile, molecular docking effectively explored their mechanism through formed hydrogen bonds and hydrophobic regions. The four peptides showed better DPP-IV inhibitory activity stability with heating treatment, pH (1-10) treatment, and in vitro gastrointestinal digestion. Our results demonstrated that the protein hydrolysate from discarded P. vannamei head can be considered as a promising natural source of DPP-IV inhibitor for helping to improve glycaemic control in Type 2 diabetes.