Purification and characterisation of antioxidative peptides from enzymatic hydrolysates of venison protein

To prepare antioxidative peptides from venison protein hydrolysates (APVPH), six proteases were employed for enzymatic hydrolysis, and the antioxidative activities of the hydrolysates were investigated using a free radical scavenging assay. Among the hydrolysates, papain hydrolysates which had the highest free radical scavenging activity were further separated into four groups and purified using consecutive chromatographic methods. Finally, two antioxidative peptides were obtained, and their sequences identified as Met-Gln-Ile-Phe-Val-Lys-Thr-Leu-Thr-Gly (APVPH I) and Asp-Leu-Ser-Asp-Gly-Glu-Gln-Gly-Val-Leu (APVPH II). The free radical scavenging activity of APVPH I was higher than that of APVPH II, and the IC50 values of the hydroxyl, DPPH, superoxide, and peroxyl radical scavenging activities were 44, 77, 217, and 85 μg/ml, respectively. These results indicate that enzymatic hydrolysates of venison protein possess potent antioxidative activity.