Journal
FOOD CHEMISTRY
Volume 168, Issue -, Pages 662-667Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2014.07.117
Keywords
Croceine croaker (Pseudosciaena crocea); Protein hydrolysate; Peptide; Antioxidant activity
Funding
- National Natural Science Foundation of China [81001393]
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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.
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