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

被引：224

作者：

Wang, Bin ^{[1
]}

Li, Li ^{[1
]}

Chi, Chang-Feng ^{[2
]}

Ma, Jia-Hui ^{[1
]}

Luo, Hong-Yu ^{[1
]}

Xu, Yin-feng ^{[1
]}

机构：

[1] Zhejiang Ocean Univ, Sch Food & Pharm, Zhoushan 316004, Peoples R China

[2] Zhejiang Ocean Univ, Sch Marine Sci, Natl Engn Res Ctr Marine Facil Aquaculture, Zhoushan 316004, Peoples R China

来源：

FOOD CHEMISTRY | 2013年 / 138卷 / 2-3期

基金：

中国国家自然科学基金;

关键词：

Blue mussel (Mytilus edulis); Protein hydrolysate; Peptide; Antioxidant activity; RADICAL-SCAVENGING ACTIVITIES; AMINO-ACIDS; OXIDATION; MUSCLE; IDENTIFICATION; FRACTIONS; GIGAS;

D O I：

10.1016/j.foodchem.2012.12.002

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

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 EC50 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. (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：1713 / 1719

页数：7

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