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

•Antioxidant hydrolysate from croceine croaker muscle (CCH-S) was obtained.•Three peptides with high antioxidant activities were isolated from CCH-S.•The sequences of peptides were determined as VLYEE, YLMSR and MILMR.•The antioxidant activities of purified peptides were evaluated by five methods.•The activities of peptides were due to smaller size and hydrophobic amino acids. 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 662.92Da, respectively. PC-1 exhibited the highest scavenging activities on DPPH (EC50 1.35mg/ml), superoxide (EC50 0.450mg/ml), and ABTS (EC50 0.312mg/ml) radicals, but PC-2 exhibited the strongest hydroxyl radical scavenging activity (EC50 0.353mg/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.