萝卜CBPs溶菌酶活性的稳定性研究  

Stability of Lysozyme Activity of Chitin-Binding Proteins from Raphanus sativus

作　　者：赖晓芳[1] 沈善瑞[1] 王炜军[2] 徐凤彩[2] 

机构地区：[1]淮海工学院海洋学院,江苏连云港222005 [2]华南农业大学生命科学学院,广州510642

出　　处：《湖北农业科学》2013年第6期1330-1333,共4页Hubei Agricultural Sciences

基　　金：江苏省海洋生物技术重点建设实验室开放基金项目(2008HS019);淮海工学院博士启动基金项目(KQ11010);淮海工学院自然科学基金项目(KX11111)

摘　　要：植物溶菌酶是植物防御体系中的一部分,在植物防卫体系中具有重要作用。萝卜中有2个具溶菌酶活性的几丁质结合蛋白(Chitin-binding proteins,CBPs),分别是CBP1、CBP2组分。为了解CBPs的作用机制以及在萝卜中的生理功能,试验研究了CBP1、CBP2溶菌酶组分酶活性的稳定性。结果显示,CBP1、CBP2在pH 5.4、65℃条件下迅速失活,在pH 3.4～10.6、25℃条件下较稳定;CBP1较CBP2对氧化剂H2O2、NaClO敏感;CBP2较CBP1对木瓜蛋白酶敏感;2个组分对胰蛋白酶均敏感。Plant lysozyme played an important role in plant defense.There are two chitin-binding proteins(CBP) with lysozyme activity purified from Raphanus sativus L.which were named as CBP1 and CBP2.The stability of lysozyme activity of CBPs was studied to understand the catalysis mechanism and physiology function of CBPs.Results showed that CBPs were stable at 25 ℃ in pH 3.4～10.6 and inactive quickly at 65 ℃ in pH 5.4;CBP1 was more sensitive to H2O2 and NaClO and less sensitive to papain than CBP2;Both CBP1 and CBP2 were sensitive to trypsin.

关 键 词：萝卜 溶菌酶活性 几丁质结合蛋白 稳定性 

分 类 号：S[农业科学]