海藻糖合酶的分离纯化及部分酶学性质  

Purification and Characterization of Trehalose Synthase Enzyme

作　　者：尚宏丽[1] 崔琰[1] 林英[1] 陈红漫[1] 

机构地区：[1]沈阳农业大学生物技术学院,辽宁沈阳110160

出　　处：《化学与生物工程》2005年第12期14-16,28,共4页Chemistry & Bioengineering

基　　金：辽宁省自然科学基金(2040515)

摘　　要：用硫酸铵沉淀、凝胶过滤层析、离子交换层析对一株芽孢杆菌SH-110产生的海藻糖合酶粗酶液进行纯化,用PAGE电泳逐步分析纯化的结果,用SDS-PAGE电泳证明该酶的分子量为62.4 kD。酶反应最适pH值为7.0,最适作用温度为35℃,金属离子Zn2+、K+、Na+对酶活性有激活作用,Ba2+、Ca2+、Mn2+对酶活性有抑制作用。酶底物专一性初步分析结果表明,该酶确实是以麦芽糖为专一性底物来转化生成海藻糖的海藻糖合酶的一种新酶。A Bacillus sp. SH-110 could produce trehalose synthase enzyme. The enzyme was purified to homogeneity by a combination of ammonium sulfate precipitation,Sephadex G-150 gel filtration and DEAE-cellulose-exchange chromatograph. The purity of every step was determined by PAGE. The enzyme molecular mass was 62.4 kD as determined by SDS-PAGE. The optimum pH value was 7.0, the optimum reaction temperature was 35℃,Zn^2＋ ,K^＋ ,Na^＋ into the reaction system increased the enzyme activity,Ba^2＋ ,Ca^2＋ ,Mn^2＋ into the reaction system decreased the enzyme activity. Prelimimary analysis on substrate specificity showed that maltose was just the Substrate specificity. This enzyme was indeed a new trehalose synthase enzyme.

关 键 词：海藻糖合酶 分离纯化 酶学性质 

分 类 号：Q533[生物学—生物化学]