堇叶碎米荠低聚肽制备工艺优化及结构特征、氧化活性研究OACSTPCD

Objective:This study aimed to prepare oligopeptidess of Camelina violifolia and expand its application range.Methods:C.violifolia protein was hydrolyzed by alkaline protease,and then used ultrafiltration membrane for isolating and concentrating,and obtained oligopeptides by freeze-drying.The structure and antioxidant activity of C.violifolia oligopeptides were analyzed.Results:The optimum conditions for the hydrolysis of C.violifolia protein were as follows:hydrolysis temperature 50 ℃,pH 10,enzyme dosage 4％,substrate concentration 2％,and hydrolysis degree 17.9％.The C.violifolia oligopeptides contents of protein and polypeptide were 49.01％and 42.87％,respectively.The oligopeptides had a strong absorption band at 200～220 nm,amide bond-specific absorption peaks,β-angle was the main secondary structure,and a 90％relative molecular weight of less than 1 000 Da.When the oligopeptides concentration was 20 mg/mL,the scavenging rates of hydroxyl radical,ABTS radical and DPPH radical were 84.54％,98.22％and 60.33％respectively.Conclusion:The preparation process of the oligopeptides of C.violifolia is reasonable and feasible.The oligopeptides have good antioxidant capacity.