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

• Published in: Food chemistry 2013-06, Vol.138 (2-3), p.1713-1719
• Main Authors: Wang, Bin, Li, Li, Chi, Chang-Feng, Ma, Jia-Hui, Luo, Hong-Yu, Xu, Yin-feng
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; amino acid sequences; amino acids; Animals; Antioxidant activity; Antioxidants - chemistry; Antioxidants - isolation & purification; Biological and medical sciences; Blue mussel (Mytilus edulis); Fish and seafood industries; Food industries; free radical scavengers; Fundamental and applied biological sciences. Psychology; hydrolysates; hydrolysis; hydroxyl radicals; linoleic acid; Lipid Peroxidation; Marine; Molecular Sequence Data; molecular weight; Mytilus edulis; Mytilus edulis - chemistry; papain; pepsin; Peptide; Peptide Mapping; Peptides - chemistry; Peptides - isolation & purification; Protein hydrolysate; protein hydrolysates; Protein Hydrolysates - chemistry; proteins; reversed-phase high performance liquid chromatography; subtilisin; superoxide anion; ultrafiltration
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2012.12.002

► Antioxidant hydrolysate of blue mussel proteins was obtained by using neutrase. ► Peptide (BNH-P7) was prepared by using ultrafiltration, gel filtration and RP-HPLC. ► The structure of BNH-P7 was determined as YPPAK (Tyr-Pro-Pro-Ala-Lys). ► BNH-P7 showed high radicals scavenging and lipid peroxidation inhibition activities. ► The high activity of BNH-P7 was due to the smaller size and Tyr and Pro residues. 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 574Da. BNH-P7 exhibited good scavenging activity on DPPH radical, hydroxyl radical, and superoxide anion radical with EC50 of 2.62, 0.228, and 0.072mg/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.