Isolation, purification, and study of certain properties of diacetyl(acetoin) reductase in the yeast Saccharomyces vini.

A V Kavadze, A K Rodopulo, G L Shaposhnikov
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Abstract

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.

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酵母菌双乙酰还原酶的分离纯化及某些性质的研究。
从酵母菌(Saccharomyces vini)的无细胞提取物中分离出一种高活性的双乙酰还原酶制剂。由于在65倍纯化过程中,2,3-丁二醇脱氢酶和二乙酰(乙酰)还原酶的活性比几乎没有变化,因此可以假设酵母细胞中含有一种酶,它既能催化NAD将2,3-丁二醇可逆氧化为乙酰,又能催化NAD- h2将二乙酰还原为乙酰。研究了该酶的一些性质。
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