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

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• 作者：Bin Wang^a ; ^{wangbin4159@hotmail.com} ; Li Li^a ; Chang-Feng Chi^b ; Jia-Hui Ma^a ; Hong-Yu Luo^a ; Yin-feng Xu^a
• 关键词：Blue mussel (Mytilus edulis) ; Protein hydrolysate ; Peptide ; Antioxidant activity
• 刊名：Food Chemistry
• 出版年：2013
• 出版时间：1 June, 2013
• 年：2013
• 卷：138
• 期：2-3
• 页码：1713-1719
• 全文大小：557 K

文摘

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.