摘要
利用自行筛选、鉴定的AcetobacterZ127,纯化出高活性的乙醇脱氢酶,并对该酶的生化特性进行了初步研究.试验表明:粗酶液通过硫酸铵分级沉淀、透析脱盐、Sephadex G-100层析分离,纯化出一种以NAD+为辅酶的ADH,经SDS-PAGE电泳检测其分子量为28KDa;ADH反应的最适pH值为7.0,最适温度为60℃,K+离子对其酶活有促进作用,二价金属离子对其活性有抑制作用,Fe3+极易使ADH产生沉淀.研究为ADH的应用及其新用途的探索提供了理论基础和可靠的工艺参数.
Using the Acetobacter Z127 which is separated and selected by ourselves, we obtained the purified and High ADH activity Acetobacter alcohol dehydrogenase （ADH）. Especially, we studied its bio-chemical property. The results showed：By using Sephadex G - 100 filtration chromatography and sodium dodecyl sulfate polyacrylamide gel electrphoresis,we got the purified 28KDa homogeneous ADH strap; Its optimum pH value and temperature is 7.0 and 60 ℃, Respectively K ^＋ has a stimulative effect and divalent metal ion has a restrain effect on ADH. It is highly unstable in Fe^3＋ solution. In a Result, this research provided credible gists for the application and the new using exploration of the alcohol dehydrogenase.
出处
《重庆大学学报（自然科学版）》
EI
CAS
CSCD
北大核心
2006年第4期65-68,共4页
Journal of Chongqing University
关键词
乙醇脱氢酶
醋酸杆菌
纯化
alcohol dehydrogenase
acetobacter
purification
