作　　者： ; ; ; ;

机构地区： 华南理工大学轻工与食品学院

出　　处： 《食品与发酵工业》 2007年第2期42-45,共4页

摘　　要： 研究了枯草杆菌蛋白酶(Subtilisin)对大豆胰蛋白酶抑制剂(STI)酶解活性的影响。实验在50℃,pH7.5条件下反应1h,并以BAPNA为底物,采用改进的方法测定枯草杆菌蛋白酶对大豆胰蛋白酶抑制剂的水解钝化程度,用SDS-PAGE方法和分子排阻色谱法研究其蛋白酶钝化敏感性。结果证明,枯草杆菌蛋白酶可以水解大部分的抑制剂,并通过SDS-PAGE进一步证实了比色法得出的结论。而由分子排阻色谱图可以分析得出抑制剂经枯草杆菌蛋白酶酶解后,活性降低。分析认为,可能是由于抑制剂中二硫键被打断使得其结构发生改变,同时生成大量复杂的小分子多肽物质。因此,可以推断大豆胰蛋白酶抑制剂的稳定性与二硫键的存在有关。 The aim of this paper was to study the inactivating of STI conducted by Subtilisin. Cubing at 50℃, pH 7. 5, the STI was treated by subtilisin and the reaction lasted about lh. Then it was measured by an improved BAPNA method after the STI was deactivated. The change of STI and the molecular weight of reactive STI were determined by size exclusive chromatographic （SEC） and SDS-PAGE, respectively. The results revealed that STI could be inactivated or hydrolyzed mostly by subtilisin, which also could be received by SDS-PAGE. Then by SEC, it seemed that the disulfide bonds of STI were unfolded, the structure of STI was changed, and lots of unknown small molecular weight compounds were made. Therefore, the stability of STI had relation to exist of disulfide bonds.

关 键 词： 大豆胰蛋白酶抑制剂 枯草杆菌蛋白酶 水解 钝化

领　　域： [轻工技术与工程] [轻工技术与工程]