烟碱脱氢酶的纯化及性质研究  

Study on the purification and properties of nicotine dehydrogenase

作　　者：马林[1] 崔成哲[1] 袁有贵[2] 刘艳芳[1] 

机构地区：[1]郑州轻工业学院食品与生物工程学院,郑州450002 [2]中国农业大学食品与营养工程学院,北京100083

出　　处：《工业微生物》2007年第4期41-44,共4页Industrial Microbiology

基　　金：国家自然科学基金项目"低水分活度环境角质酶协同尼古丁脱氢酶降解尼古丁机理"(20646004);国家烟草专卖局科技攻关项目"生化技术在烟草工业中的应用"(合同号:110200101039))资助

摘　　要：通过硫酸铵沉淀、离子交换层析和凝胶过滤等方法对节杆菌(ArthrobacterZ3)所产烟碱脱氢酶进行了纯化,该酶经SDS-PAGE电泳检测为一条带,分子量约为120kDa。该酶活力的最适温度为40℃,在pH5.5-8.0范围内稳定,最适pH约为7.0;对烟碱作用的Km值为7.694×10-4mol/L;Mn2+、Co2+是酶的激活剂,而Cu2+是酶的抑制剂。Nicotine dehydrogenase was purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration from the culture brothe of a strain named ArthrobacterZ3. SDS-PAGE electrophoresis of the purified fraction showed a simple band which revealed this enzyme was purificd and the molecular weight of this enzyme was 120,000. Results showed that it had the highest activity at pHT. 0 and 40℃. Dynamic studies demonstrated that it was an enzyme with Km of 7. 694 × 10^-4 mol/L. Mn^2＋ and Co^2＋ activatcd the enzyme although Cu^2＋ inhibited it.

关 键 词：节杆菌Z3 烟碱脱氢酶 纯化 特性 

分 类 号：TS41[农业科学—烟草工业]