High pressure-assisted enzymatic hydrolysis promotes the release of a bi-functional peptide from cowhide gelatin with dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant activities.

The process of generating functional peptides from cowhide gelatin is challenged by inefficient enzymatic hydrolysis. In this study, the researchers attempted to enhance the hydrolysis and potential functional properties of the peptides by subjecting the cowhide gelatin to high-pressure treatment (200, 300, and 400 MPa) for 20 min, followed by enzymatic hydrolysis. The highest 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, 2,2' azinobis(3 ethylbenzothiazoline 6 sulfonic acid) (ABTS) radical scavenging activity, and DPP-IV inhibitory activity of the hydrolysate were obtained at 200 MPa, accompanied with an increase in the content of hydrophobic, acidic, and basic amino acids (P < 0.05). Correspondingly, the high-pressure pretreatment (200 MPa) reduced the thermal stability, particle size, and morphological integrity of cowhide gelatin, with a corresponding increase in the exposure of hydrophobic regions. Altogether, these results indicated that appropriate high-pressure-assisted enzymatic hydrolysis reinforced the release of bi-functional peptides by modifying the structure of cowhide gelatin.