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采用Nagano法从豆粕中分离β-伴大豆球蛋白并酶解制备水解肽,以单因素试验和正交试验确定酶解最佳条件,通过高效液相法分析β-伴大豆球蛋白水解肽的分子量分布,比较并检测了β-伴大豆球蛋白水解肽和大豆分离蛋白水解肽的体外抗氧化效果。结果显示:在20g/L的底物浓度下的最佳条件为酶和底物比10000U/g,温度55℃,pH7.5,水解时间4h,水解度为72.7%,明显高于酶解大豆分离蛋白51.4%的水解度,且水解时间更短。β-伴大豆球蛋白水解肽主要为130～1000u的短肽,占肽总量的86.3%,均一性极高。β-伴大豆球蛋白水解肽对O2-.和.OH均有清除作用,清除.OH的能力明显高于大豆分离蛋白水解肽,即β-伴大豆球蛋白的水解肽对大豆肽清除.OH的作用贡献更大。
The Nagano method was used to separate β-conglycinin from soybean meal and hydrolyze it to prepare the hydrolyzed peptide. The optimum conditions for enzymolysis were determined by single factor test and orthogonal test. The content of β-conglycinin Molecular weight distribution, in vitro antioxidant effects of β-conglycinin and soybean proteolytic peptides were compared and tested. The results showed that under the substrate concentration of 20g / L, the optimum conditions were as follows: enzyme and substrate ratio 10000U / g, temperature 55 ℃, pH7.5, hydrolysis time 4h, hydrolysis degree 72.7% The degree of hydrolysis of the protein is 51.4% and the hydrolysis time is shorter. The β-conglycinin peptide is mainly a short peptide of 130-1000u, accounting for 86.3% of the total peptide, with very high homogeneity. β-conglycinin hydrolyzing peptide has the scavenging effect on both O2- and .OH, and the ability to scavenge OH is obviously higher than that of soybean proteolytic peptide, that is, the hydrolyzing peptide of β-conglycinin cleaves soybean peptide.OH The contribution of the role of greater.