Purification and characterization of antioxidative peptide derived from muscle of conger eel (Conger myriaster)

Abstract

The tryptic hydrolysate of conger eel (Conger myriaster) muscle protein was fractionated according to the molecular weights using ultrafiltration (UF) membrane system. The lowest molecular weight fraction (<1 kDa) with higher antioxidative properties was purified using consecutive chromatographic techniques and designated conger eel antioxidative peptide (CEAP). Sequence determination revealed that it contained nine amino acids in its sequence (LGLNGDDVN) and the molecular mass was identified to be 928 Da. CEAP performed better than the natural antioxidant, α-tocopherol for the prevention of lipid peroxidation in vitro. Additionally, it scavenged hydroxyl radicals and carbon-centered radicals at IC50 values of 74.1 μM and 78.5 μM, respectively. Therefore these results suggested that the peptides derived from conger eel protein hydrolysates are responsible for higher antioxidative properties and molecular weight as well as presence of hydrophobic amino acids highly contributed for their antioxidation.