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

Cuiling WU; Ribang WU; Dan Liu; Xinghao Yang; Jiang Zhang; Jiafeng Huang; Hailun HE

Return

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

Author: Cuiling WU ¹ ; Ribang WU ¹ ; Dan LIU ¹ ; Xinghao YANG ¹ ; Jiang ZHANG ¹ ; Jiafeng HUANG ¹ ; Hailun HE ¹
Author Information

1. State Key Laboratory of Medical Genetics, School of Life Sciences, Central South University, Changsha 410013, Hunan, China.
Publication Type:Journal Article
Keywords: Corrhinus molitorella; DNA oxidation damage; DPPH; ORAC; antioxidant peptide; collagen
MeSH: Amino Acid Sequence; Animals; Antioxidants; chemistry; Chromatography, Gel; Collagen; chemistry; Cyprinidae; Dextrans; Hydrolysis; Oxidation-Reduction; Peptide Hydrolases; Peptides; chemistry; Skin; chemistry
From: Chinese Journal of Biotechnology 2016;32(12):1727-1734
CountryChina
Language:Chinese
Abstract: In order to prepare antioxidant peptide through hydrolyzing low-value protein resources with bacterial extracellular proteases and to discover novel proteases, crude extracellular protease from Pseudoalteromonas sp. SHK1-2 was obtained through fermentation which 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.