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Grass carp muscles were hydrolyzed with various proteases (papain, bovine pancreatin 6.0, bromelain, neutrase 1.5MG and alcalase 2.4L) to extract antioxidant peptides. The hydrolysates were assessed using methods of hydroxyl radical scavenging ability and lipid peroxidation inhibition activity. Hydrolysate prepared with alcalase 2.4L was found to have the highest antioxidant activity. It was purified using ultrafiltration and consecutive chromatographic methods including ion-exchange chromatography, multilayer coil high-speed counter-current chromatography, and gel filtration chromatography. The purified peptide, as a potent antioxidant, was identified as Pro-Ser-Lys-Tyr-Glu-Pro-Phe-Val (966.3Da) using RP-HPLC connected on-line to an electrospray ionization mass spectrometry. As well, it was found that basic peptides had greater capacity to scavenge hydroxyl radical than acidic or neutral peptides and …