Preparation and identification of novel antioxidant peptides from collagen hydrolysate of sheep hoof assisted by ultrasound

In this study, different ultrasound-assisted modes [ultrasonic simultaneous (US) and ultrasonic preconditioning (UP)] of synergistic enzymatic hydrolysis were used to prepare bioactive peptides of sheep hoof collagen. The 2, 2-diphenyl - 1-picrylhydrazyl (DPPH) radical scavenging activity, 2,2 '-Azino-bis (3-ethylbenzothiazoline-6sulfonic acid) (ABTS) radical scavenging capacity and metal chelating capacity of sheep's hoof collagen antioxidant peptides (SCPs) (at 1 mg/mL) prepared at 20 min of treatment in US treatment mode (US-20) were 48.56 +/- 0.68 %, 51.97 +/- 1.15 % and 65.58 +/- 1.36 %, respectively, which were higher compared with the control and UP groups. Using LC-MS/MS analysis, 9336, 11,527, and 11,909 peptide sequences were identified from collagen hydrolysate by C, UP-20, and US-20, respectively. The peptides ACEDAPPSAAHFR and FGFEVGPACFLG with high bioactivity were screened using computer analysis. Molecular docking results revealed that hydrogen bonding and hydrophobic interactions between the two peptide sequences with DPPH and ABTS radicals may be responsible for their antioxidant properties. Therefore, we have optimized the extraction of bioactive peptides from sheep hoof collagen using ultrasound-assisted enzymatic hydrolysis, which is helpful for the high-value utilisation of sheep hoof by-products and the extraction of foodborne antioxidant peptides.