酿酒酵母乙醛脱氢酶活性检测反应体系优化  

Optimization on activity detection system of acetaldehyde dehydrogenase from Saccharomyces cerevisiae

作　　者：赵玉凤[1] 雷明科[2] 吴元欣[2] 王存文[2] 

机构地区：[1]华中农业大学生命科学技术学院农业微生物学国家重点实验室,湖北武汉430070 [2]武汉工程大学化工与制药学院湖北省新型反应器与绿色化学工艺重点实验室,湖北武汉430074

出　　处：《中国酿造》2008年第5期23-26,共4页China Brewing

基　　金：湖北省国际科技合作重点项目计划(2006CA013);湖北省科技攻关计划(2007AA201C27,2007AA301B24)

摘　　要：研究了酵母乙醛脱氢酶(ALDH)的部分酶学性质,结果表明:该酶最适pH值为8.5,PO43-对该酶没有激活作用,巯基乙醇等保护剂对该酶的测定有重要作用,该酶为依赖K+的金属酶,Mg2+、Mn2+、Zn2+有抑制作用,Ca2+、Na+有激活作用,其中Mn2+的抑制类型为反竞争性抑制,其抑制剂常数Ki为8.73×10-4mol/L。The enzymological characters of acetaldehyde dehydrogenase （ALDH） from Saccharomyces ceravisiae were studied. The results showed that the optimal pH of ALDH was about 8.5. The ALDH could not be activated by PO4^3-. The protecting agents, such as mercaptoethanol, were important for the system of activity detection. The results also showed that the ALDH was K^＋-activated dehydrogenase. The metal ions, including Mg^2＋, Mn^2＋ and Zn^2＋, could inhibit its activity, whereas Ca^2＋ and Na^＋ could activate its activity. Mn^2＋ was found to be an uncompetifive inhibition of this enzyme, with an inhibitor constant of 8.73×10^-4 mol/L.

关 键 词：乙醛脱氢酶 酶活 金属离子 

分 类 号：Q55[生物学—生物化学]