title: Purification and characterisation of a novel antioxidant peptide derived from blue mussel (Mytilus edulis) protein hydrolysate.
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.
authors: School of Food and Pharmacy, Zhejiang Ocean University, Qixiangtai Road 51, Zhoushan 316004, PR China. wangbin4159@hotmail.com
authors: Bin
authors: B
authors: Wang
authors: Li
authors: L
authors: Li
authors: Chang-Feng
authors: CF
authors: Chi
authors: Jia-Hui
authors: JH
authors: Ma
authors: Hong-Yu
authors: HY
authors: Luo
authors: Yin-feng
authors: YF
authors: Xu
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000975:Antioxidants / Q000737:chemistry* / Q000302:isolation & purification*; D015227:Lipid Peroxidation; D008969:Molecular Sequence Data; D049880:Mytilus edulis / Q000737:chemistry*; D010449:Peptide Mapping; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification*; D011492:Protein Hydrolysates / Q000737:chemistry*
chemical_list: D000975:Antioxidants; D010455:Peptides; D011492:Protein Hydrolysates