机构地区: 华南理工大学轻工与食品学院
出 处: 《食品工业科技》 2007年第3期82-84,88,共4页
摘 要: 研究了二巯基苏糖醇(DTT)、亚硫酸钠(Na2SO3)和半胱氨酸(Cys)对大豆胰蛋白酶抑制剂活性的影响。实验在温度80℃,pH7.5条件下反应,并以BAPNA为底物,采用改进的方法测定DTT对大豆蛋白酶抑制剂的钝化作用,最后用SDS-PAGE方法和凝胶排阻色谱法研究其蛋白酶钝化敏感性。通过改进的BAPNA法得出还原剂钝化大豆胰蛋白酶抑制剂由大到小顺序依次为:DTT>Na2SO3>Cys,并通过SDS-PAGE进一步证实了比色法得出的结论。而凝胶排阻色谱法说明了还原剂对大豆胰蛋白酶抑制剂作用使得抑制剂中二硫键被打断,抑制剂结构发生改变,有新的物质生成。所以,得出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 inactivation of STI by dithiothreitol (DTT). Na2SO3 and Cys . After incubation at 80℃, pH 7.5 , STI was measured by an improved BAPNA method. The changes of STI were determined by size exclusion chromatography (SEC) and SDS-PAGE, respectively, The results revealed that STI was inactivated by reducing agents. and the inhibition effectiveness was as follows: DTT〉Na2SO3〉Cys. which was also proved by SDS-PAGE. By SEC we could know that the disulfide bonds of STI were broken, and the structure of STI was changed. and some new compounds were produced. Therefore, the stability of STI is closely related to disulfide bonds.