Preparation and antioxidant activity detection of collagen peptide from Cirrhinus molitorella skin / 生物工程学报
Chinese Journal of Biotechnology
; (12): 1727-1734, 2016.
Article
in Zh
| WPRIM
| ID: wpr-243685
Responsible library:
WPRO
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.
Key words
Full text:
1
Index:
WPRIM
Main subject:
Oxidation-Reduction
/
Peptide Hydrolases
/
Peptides
/
Skin
/
Cyprinidae
/
Chemistry
/
Chromatography, Gel
/
Collagen
/
Amino Acid Sequence
/
Dextrans
Type of study:
Diagnostic_studies
Limits:
Animals
Language:
Zh
Journal:
Chinese Journal of Biotechnology
Year:
2016
Type:
Article