Purification and Identification of an Antioxidative Peptide from Digestive Enzyme Hydrolysis of Cutlassfish Muscle

Abstract

The major objective of this study was to investigate the pepsin digests of cutlassfish muscle for their antioxidant activity. The peptide isolated after 3 h of pepsin hydrolysis demonstrated the highest scavenging activity for both 1,1-Diphenyl-2-picrylhydrazyl (DPPH) and alkyl radicals. It also had the highest yield of the isolates with the highest protein content, which was likely related to its higher degree of hydrolysis than the other hydrolysates. The antioxidant peptide purified from the 3 h pepsin hydrolysate indicated the amino acid sequence, Phe-Ser-Gly-Gly-Glu. This study suggests that cutlassfish muscle is an excellent antioxidant source and could be effectively used as a food ingredient and in pharmaceuticals.