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Food Chem. 2013 Jun 1;138(2-3):1713-9. doi: 10.1016/j.foodchem.2012.12.002. Epub 2012 Dec 8.

Purification and characterisation of a novel antioxidant peptide derived from blue mussel (Mytilus edulis) protein hydrolysate.

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  • 1School of Food and Pharmacy, Zhejiang Ocean University, Qixiangtai Road 51, Zhoushan 316004, PR China. wangbin4159@hotmail.com

Abstract

Protein derived from blue mussel (Mytilus edulis) was hydrolysed using four kinds of proteases (pepsin, papain, neutrase and alcalase), and the neutrase hydrolysate (BNH) obtained by 3-h hydrolysis exhibited the highest 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity compared to other hydrolysates. By using ultrafiltration, gel filtration chromatography and reversed phase high performance liquid chromatography (RP-HPLC), a novel antioxidant peptide (BNH-P7) was isolated from BNH, and its amino acid sequence was identified as YPPAK (Tyr-Pro-Pro-Ala-Lys) with molecular weight of 574 Da. BNH-P7 exhibited good scavenging activity on DPPH radical, hydroxyl radical, and superoxide anion radical with EC(50) of 2.62, 0.228, and 0.072 mg/ml, respectively. BNH-P7 was also effectively against lipid peroxidation in a linoleic acid model system. The high activity of BNH-P7 was due to the small size and the presence of antioxidant and hydrophobic amino acid residues (Tyr and Pro) within its sequence.

Copyright © 2012 Elsevier Ltd. All rights reserved.

PMID:
23411302
[PubMed - indexed for MEDLINE]
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