PMID: 45079May 1, 1979

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

Biology Bulletin of the Academy of Sciences of the USSR
A V KavadzeG L Shaposhnikov


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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