Study On The Preparation Of Sturgeon Skin Collagen Peptides By Enzymatic Method And Its Antioxidant Activity
Keywords
Sturgeon Skin, Collagen Peptide, Alkaline Protease, Enzymatic Hydrolysis, Antioxidant Activity
Abstract
Abstract This study used sturgeon skin as raw material and used alkaline protease hydrolysis to prepare collagen peptides. The basic components of sturgeon skin were analyzed, the enzymatic hydrolysis conditions were optimized, and the antioxidant activity of the enzymatic hydrolysis products was studied. The results showed that the optimal enzymatic hydrolysis conditions were pH 9, temperature 55¡ãC, added enzyme mass fraction 3%, and the degree of hydrolysis was 22.0% when the enzymatic hydrolysis time was 5 h. The enzymatic hydrolyzate was separated by ultrafiltration to obtain four collagen peptide components with different molecular mass ranges: SSCP-I (molecular mass >10 000 Da), SSCP-II (molecular mass = 5 000~10 000 Da), and SSCP-¢ó (Molecular mass = 1 000~5 000 Da) and SSCP-IV (Molecular mass <1 000 Da). Among them (molecular mass = 1 000~5 000 Da) SSCP-¢ó has the highest scavenging ability for superoxide anion radicals, and its half-inhibitory scavenging concentration IC50 is 5.938 g/L. This research provides theoretical guidance for the comprehensive processing and high-value utilization of sturgeon skin. For further information of this article and research, feel free to contact our team for asssitance. Original research was done by Zhu Yougui, Wang Zhao, Wang Shengfan, Zhang Yinjun, Zheng Jianyong, Li Luyuan
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