作　　者： ; ;

机构地区： 华南理工大学轻工与食品学院食物蛋白工程研究中心

出　　处： 《食品与发酵工业》 2009年第11期144-147,151,共5页

摘　　要： 通过Nagano方法制备得纯度达95%以上的大豆球蛋白,以其为原料,通过制备型液相色谱,对大豆球蛋白的组成多肽进行了分离。结果显示:以DEAE-Sepharose Fast Flow为分离介质,以含有6 mol/L碳酰二胺和0.02 mol/L巯基乙醇、pH值为6.45的0.05 mol/L磷酸缓冲液为平衡液,通过对穿透液及梯度洗脱液的分部收集,大豆球蛋白的组成多肽能得到较好的分离,回收率达到75%,聚丙烯酰胺凝胶电泳显示各组分的纯度达90%。此外,对各组成多肽的氨基酸组分及种类进行了分析。 Soybean glycinin with a purity above 95% was isolated by Nagano method. Separation of the polypeptides from glycinin was obtained by DEAE-Sepharose chromatography. The equilibrated balance solution was made by 0.05 M phosphate buffer （ pH 6.45） which contained 6.0 M urea and 0.1M 2 - ME. Individual polypeptides of glycinin was well separated in the collecting of the liquid penetrating with the gradient eluting. The overall recovery of to- tal fractions was almost 75% , and the purity for each polypeptides was more than 90% measured by polyacrylamide gel electrophoresis. In addition, the amino acid compositions of individual polypeptides and their analysis.

关 键 词： 大豆球蛋白 多肽 分离 制备型液相色谱 氨基酸组分分析

领　　域： [轻工技术与工程] [轻工技术与工程] [农业科学] [轻工技术与工程] [轻工技术与工程]