Abstract:The low-cost laver was hydrolyzed with neutral protease and aminopeptidase in this study.The antioxidative peptides were purified initially by adding 60%ethanol to remove polysaccharides in the hydrolysate.The supernatant was further purified through Sephadex G-10 gel,DEAE-52 anion-exchange and SOURCE 3RPC to get more purer enzymatic laver antioxidative peptides(ELAP).The scavenging activities of Superoxide-radical,DPPH radical and Hydroxyl -radical were 23.25%,47.12%and 47.12%respectively when the content of the ELAP was at 100μg/mL.Compared to vitamin C at the same content(100μg/mL),the scavenging activities in the ELAP were 0.79,0.87 and 0.91 times of the activities in vitamin C,Furthermore, the reducing ability of the low-cost laver peptides was 1.23 times than that of vitamin C. According to the chromatographic of analytical reverse-phase high performance liquid chromatography (RP-HPLC).the purity of ELAP was up to 87.44%.The ELAP was identified as a hexapeptide AGVGTG(Asp-Gly-Val-Gly-Tyr-Gly) with analysis of the ultra-performance liq- uid chromatography-quadrupole time-of-flight mass spectrometry(Q-TOF-MS).The composition of the hexapeptideC AGVGTG) in the ELAP which contained Tyr and Gly has the typical function of antioxidation.
