Purification and characterization of three antioxidant peptides from protein hydrolyzate of croceine croaker (Pseudosciaena crocea) muscle

卷:168

Chi, Chang-Feng ; Hu, Fa-Yuan ; Wang, Bin ; Ren, Xi-Jie ; Deng, Shang-Gui ; Wu, Chang-Wen

Zhejiang Ocean Univ

关键词: Croceine croaker (Pseudosciaena crocea);    Protein hydrolysate;    Peptide;    Antioxidant activity;   

DOI  :  10.1016/j.foodchem.2014.07.117

学科分类：食品科学和技术

【 摘 要 】

Three antioxidant peptides were purified from protein hydrolysate of croceine croaker (Pseudosciaena crocea) muscle prepared using pepsin and alcalase, and identified as Tyr-Leu-Met-Ser-Arg (PC-1), Val-Leu-Tyr-Glu-Glu (PC-2), and Met-Ile-Leu-Met-Arg (PC-3) with molecular weights of 651.77, 668.82, and 662.92 Da, respectively. PC-1 exhibited the highest scavenging activities on DPPH (EC50 1.35 mg/ml), superoxide (EC50 0.450 mg/ml), and ABTS (EC50 0.312 mg/ml) radicals, but PC-2 exhibited the strongest hydroxyl radical scavenging activity (EC50 0.353 mg/ml) among the three peptides. PC-1 also showed effective inhibition on lipid peroxidation in the model system. The good activities of isolated peptides might be benefit from the smaller size and hydrophobic and/or aromatic amino acids within their sequences. (C) 2014 Elsevier Ltd. All rights reserved.