【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。更多还原

【Abstract】 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 purified and the molecular weight of this enzyme was 120,000.Results showed that it had the highest activity at pH7.0 and 40℃.Dynamic studies demonstrated that it was an enzyme with Km of 7.694×10-4 mol/L.Mn2+ and Co2+ activated the enzyme although Cu2+ inhibited it.更多还原