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.
出处
《工业微生物》
CAS
CSCD
北大核心
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
关键词
节杆菌Z3
烟碱脱氢酶
纯化
特性
ArthrobacterZ3
nicotine dehydrogenase
purification
properties
