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Corresponding Author(s)

向极钎（1967—），男，恩施土家族苗族自治州农业科学院研究员。E-mail: hmxjq@163.com

Abstract

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.

Publication Date

1-30-2024

First Page

189

Last Page

196

DOI

10.13652/j.spjx.1003.5788.2023.80318

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