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Isolation, purification, and study of certain properties of diacetyl(acetoin) reductase in the yeast Saccharomyces vini.
Metadata
JournalBiol Bull Acad Sci USSRNot FoundDate
1979-May-Jun
Type
Journal Article
Volume
1979-May-Jun / 6 : 356-61
Author
Kavadze AV , Rodopulo AK , Shaposhnikov GL
Doi
Not Found
PMIDMESH
Acetoin Dehydrogenase
Alcohol Oxidoreductases
Butylene Glycols
Chromatography, Ion Exchange
Hydrogen-Ion Concentration
Isoelectric Focusing
Protein Conformation
Saccharomyces
Temperature
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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Biol Bull Acad Sci USSRBiology bulletin of the Academy of Sciences of the USSR
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