作　　者： ; ; ; ;

机构地区： 华南理工大学轻工与食品学院

出　　处： 《华南理工大学学报（自然科学版）》 2006年第8期105-109,共5页

摘　　要： 研究了大豆分离蛋白(SPI)的枯草杆菌蛋白酶水解产物的聚集作用,以及参与聚集组分的氨基酸组成及其相互作用.十二烷基磺酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)和SE-HPLC分析显示,SPI的枯草杆菌蛋白酶降解产物大部分为分子质量小于6.5 ku的小分子组分,聚集物主要由这些小分子组分组成.聚集物可溶于脲素、盐酸胍或SDS,而难溶于β-巯基乙醇.氨基酸分析显示聚集物中的疏水性氨基酸含量高于SPI.说明疏水相互作用是聚集物形成的主要推动力,氢键、静电引力参与稳定聚集物的结构,而二硫键很少参与聚集物的形成.文中还从蛋白质分子结构的角度,探讨了SPI的枯草杆菌蛋白酶水解多肽的聚集机理. The aggregation of the hydrolysates of soy protein isolate （SPI） induced by subtilisin protease was investigated. The amino acid composition of the aggregates and the interaction involved in the aggregation was also discussed. It is indicated by the SDS-PAGE （Sodium Dodecyl Sulphate-Polyacrylamide Gel Electropharesis） and the SE-HPLC （Size Exclusion-High Performance Liquid Chromatography） analyses that SPI is digested to small fragments with the molecular mass less than 6.5 ku, which are the major fragments involved in the aggregates. Moreover, the obtained aggregates can be solubilized in buffers such as urea, guanidine hydrochloride and SDS, but can hardly solubilized in β-mercaptoethanol. As revealed by the amino acid analysis, the content of the hydrophobic amino acid in the aggregates is greater than that in SPI, which suggests that （l） the hydrophobic interaction force is the major force to drive the aggregation; （2） hydrogen bonds and electrostatic forces play a role in the stabilization of the finally-formed aggregates; and （3） disulfide bonds hardly contribute to the aggregation. The mechanism of the aggregation of the peptides derived from SPI induced by subtilisin protease is also discussed in this paper in terms of the molecular structure of protein.

关 键 词： 大豆分离蛋白 枯草杆菌蛋白酶 聚集 相互作用 机理

领　　域： [轻工技术与工程] [轻工技术与工程]