Preparation and antioxidant activity detection of collagen peptide from Cirrhinus molitorella skin

Abstract:

We prepared antioxidant peptide through hydrolyzing low-value protein resources with bacterial extracellular proteases and to discovered novel proteases. Crude extracellular protease obtained from Pseudoalteromonas sp. SHK1-2 fermentation was used to hydrolyze collagen extracted from Cirrhinus molitorella skin. Small peptide fraction was isolated from hydrolysate by ultrafiltration and Sephadex LH-20 size exclusion chromatography and showed 1, 1-diphenyl-2-picrylhydrazyl radical scavenging activity (35.6%±7%), oxygen radical absorbance capacity and inhibition of DNA oxidation damage. The molecule weight was 776.2 Da, and amino acid sequence was Thr-Ala-Gly-His-Pro- Gly-Thr-His through liquid chromatography mass spectrum. Our findings suggest that peptide obtained from low-value protein of fish waste by hydrolysis with bacterial protease has antioxidant activity.