Kavadze A V, Rodopulo A K, Shaposhnikov G L
Biol Bull Acad Sci USSR. 1979 May-Jun;6(3):356-61.
A highly active preparation of diacetyl(acetoin) reductase was isolated from cell-free extracts of the yeast Saccharomyces vini. Since the activity ratio of 2,3-butanediol dehydrogenase and diacetyl(acetoin) reductase was practically unchanged in the process of 65-fold purification, it can be assumed that the yeast cells contain one enzyme, which catalyzes both the reversible oxidation of 2,3-butanediol to acetoin by NAD and the practically irreversible reduction of diacetyl to acetoin by NAD-H2. Some properties of this enzyme were studied.
从葡萄酒酵母(Saccharomyces vini)的无细胞提取物中分离出了一种高活性的双乙酰(乙偶姻)还原酶制剂。由于在65倍纯化过程中,2,3-丁二醇脱氢酶和双乙酰(乙偶姻)还原酶的活性比几乎没有变化,因此可以假定酵母细胞含有一种酶,该酶既能催化由NAD将2,3-丁二醇可逆氧化为乙偶姻,又能催化由NAD-H2将双乙酰几乎不可逆地还原为乙偶姻。对这种酶的一些特性进行了研究。