Purification of antioxidative peptide from peptic hydrolysates of Mideodeok (Styela clava) flesh tissue

Abstract

In this study, an antioxidative peptide was obtained by hydrolyzation of mideodeok (Styela clava) flesh tissue with various proteases and purified through gel filtration chromatography and reverse phage-HPLC (RPHPLC), and then antioxidant activity was investigated using electron spin resonance (ESR) spectrometer. Among the enzymatic hydrolysates, the peptic hydrolysate exhibited the highest antioxidant activity, and a strong antioxidant peptide was purified from the hydrolysate. The peptide sequence, Leu-Trp-His-Thr-His (692.2 Da), was identified by quardruple time-of-flight electrospray ionization (QTOF ESI)-MS. This antioxidative peptide strongly scavenged peroxyl radical with the IC50 value of 39.4 mu M.