家蚕表皮多酚氧化酶的分离纯化及酶学性质研究  

Study on the Separation,Purification and Enzymatic Properties of Polyphenoloxidase from Epidermis of Bombyx mori

作　　者：马晓春[1] 韩宏岩[1] 许维岸[1] 

机构地区：[1]苏州大学基础医学与生物科学学院,江苏苏州215123

出　　处：《安徽农业科学》2009年第17期7870-7871,共2页Journal of Anhui Agricultural Sciences

摘　　要：[目的]分离纯化家蚕多酚氧化酶,并对其性质进行分析研究。[方法]采用硫酸铵分级沉淀、凝胶过滤、蛋白质电泳等方法。[结果]多酚氧化酶分子量约为81 kD;最适温度为30℃;最适pH值为7.0。低浓度金属离子Ag+、Cu2+、Mn2+、Zn2+对多酚氧化酶有一定的激活作用,而高浓度有抑制作用。[结论]金属离子对家蚕多酚氧化酶的影响很大,值得更深入的研究。[ Objective] The research aimed to separate and purify polyphenoloxidase from Bombyx mori and study its properties. [ Method ] The methods of ammonium sulfate precipitation, gel filtration, protein electrophoresis and so on were used. [ Result] The molecular weight of polyphenoloxidase was about 81 kD. The optimum temperature was 30 ℃ and the optimun pH was 7.0. The metal iota of Ag^＋, Cu^2＋, Mn^2＋ and Zn^2＋ at low concentration had certain activation on polyphenoloxidase and that at high concentration had inhibition. [ Conclusion] The influences of heavy metal ions on polyphenoloxidase from Bombyx mori were greater, to be worth htrther study.

关 键 词：家蚕 多酚氧化酶 分离纯化 性质 

分 类 号：S188[农业科学—农业基础科学]