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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.


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.

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