Purification and identification of an antioxidative peptide from peony (Paeonia suffruticosa Andr.) seed dreg.

The present study demonstrated the hydrolysis of peony seed protein isolate (PSPI) by using alcalase and resulted in the generation of an anti-oxidative peptide. In brief, a model was used to illustrate the enzymolysis of PSPI with the determination of kinetic factors as per investigation information. The model proved suitable to explain the PSPI hydrolysis by alcalase. A novel anti-oxidative peptide was obtained successfully by ultrafiltration and a series of chromatography techniques. Subsequently, a purified fragment was identified with the amino acid sequence of SMRKPPG followed by its synthesis and evaluation of its anti-oxidative activities. After hydrolysis, the peony seed protein hydrolysate (PSPH) with the degree of hydrolysis of 18% displayed the most significant antioxidant action which was further used to isolate the anti-oxidative peptide.