Isolation, purification, and study of certain properties of diacetyl(acetoin) reductase in the yeast Saccharomyces vini.
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.
D000094:Acetoin Dehydrogenase / Q000032:analysis* / Q000302:isolation & purification; D000429:Alcohol Oxidoreductases / Q000032:analysis*; D002072:Butylene Glycols / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D011487:Protein Conformation; D012440:Saccharomyces / Q000201:enzymology*; D013696:Temperature
D002072:Butylene Glycols; D000429:Alcohol Oxidoreductases; D000094:Acetoin Dehydrogenase