乙醇脱氢酶的初步分离及其酶学性质的研究  

Study on Primary Separation and Enzymatic Properties of Alcohol Dehydrogenase

作　　者：吴桂英[1] 金放[2] 吴元欣[2] 赵玉凤[2] 

机构地区：[1]黄石理工学院化学与材料工程学院,湖北黄石435003 [2]武汉工程大学化工与制药学院,湖北武汉430073

出　　处：《化学与生物工程》2009年第6期69-71,共3页Chemistry & Bioengineering

摘　　要：以硫酸铵为沉淀剂,采用盐析法对乙醇脱氢酶（ADH）进行了初步的分离纯化,ADH比活力从粗酶液的0.464 U·mg^-1提高到1.198 U·mg^-1,纯化倍数为2.582。研究了ADH的基本酶学性质,其最适作用pH值为7.0-10.0,pH值为8.0时酶活力达到最大,pH值为7.0时酶较为稳定;最适作用温度为37℃,温度为30-40℃时酶活力较为稳定,温度超过45℃后酶活力急剧下降。The alcohol dehydrogenase （ADH） was primarily separated and purified by the salting out method with ammonium sulfate as precipitant. The ADH activity was improved from 0. 464 U ·mg^-1 of crude enzyme liquid to 1. 198 U·mg^-1 and purified multiplier was 2. 582. Study results on the enzymatic properties of ADH showed that the maximum activity of ADH was obtained at 37℃ and pH value 8.0, and it was quite stable at pH value 7.0 and at 30-40℃,but its enzymatic activity sharply declined when the temperature was over 45℃.

关 键 词：乙醇脱氢酶 分离 酶学性质 

分 类 号：Q554.9[生物学—生物化学]