Abstract
The present study focused on the effects of different preparation conditions on the activity and peptide sequence identification of DPP-IV inhibitory peptides based on discarded cowhide collagen and its regulation mechanism. The highest DPP-IV inhibitory activity (IC50 of 3.04 ± 0.13 mg/mL) was obtained by the combination of double enzymatic hydrolysis (papain and compound protease) and optimized IL-US (ultrasound-assisted ionic liquids) pretreatment. The optimal pretreatment condition for ultrasonic power, ultrasonic time, ionic liquid/collagen ratio, and collagen concentration were 389 W, 25 min, 0.7, and 0.3 %, respectively. IL-US pretreatment induced the exposure of active sites and hydrophobic amino acids of collagen peptide, promoted the partial transformation of β-sheet to β-turn, and enhanced the stability of gastrointestinal digestion. Seven new peptides with DPP-IV inhibitory ability were identified. Importantly, further molecular docking showed that five peptides (GPVG, FGPGP, APGGAP, GPPGPT, and GPVGPPG) were proposed to be antidiabetic peptides from cowhide collagens.
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