| During the past decades, the antioxidative peptide is on going a hot spot. In the present paper, the proteast screening and the response surface optimization were performed. Accordingly, the hydrolysate containing the high antioxidative peptides were successfully obtained. Simulteneously, its antioxidative properties in vivo and vitro were investigated. Our results confirm that the protamex is the ideal enzyme tool comparied to the other three proteasts, whose optimal enzymatic hydrolysis conditions is pH7.49,49.59℃and3.02h for this study. Using this hydrolysis conditions, the corresponding hydrolysate have a high antioxidative ability, whose clearance rate of DPPH can hit95.07%. Futhermore, IC50of the hydrolysate was detected. The results show that the values of IC50of hydrolysate for superoxide anion and DPPH are7.97mg/ml and2.89mg/ml, respectively. According to the animal experiments, the white mouse who were gavaged with low-dosage,middle-dosage and high-dosage enzymatic hydrolysates respectively,showed a significant different with the standard chow in CAT, SOD and MDA (p<0.05).It showed that the hydrolysates could decrease the content of MDA by57.4%and increase the activities of CAT and SOD by20.1%and4.2%, respectively. As a result, the conclusion can be drawn that the hydrolysates obtained possessed high antioxidative ability both in vivo and in vitro.The enzymatic hydrolysates were separated into different molecular weight by the method of ultrafiltration. The invitro antioxidant activity of the enzymatic hydrolysates was studied. The results indicate:the molecular weight of hydrolysates which below3kDa maintained the optimum activity. The DPPH radical clearance rate of that with the concentration of8mg/mL was94.9%. The objective enzymatic hydrolysates were separated by Sephadex G-25and the molecular weight was measured. The target hydrolysates were separated into three constituents by Sephadex G-25, which are298IDa,2561Da and1335Da respectively. |
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