Separation and properties of two acetylacetoin reductases from Bacillus cereus YUF-4.
The separation and purification of two kinds of acetylacetoin reductases (AACRs) from Bacillus cereus YUF-4 were examined. NADPH-linked AACR (AACR I) and NADH-linked AACR (AACR II) were separated from each other by ammonium sulfate fractionation, DEAE-cellulose chromatography, and hydroxyapatite chromatography. The former was purified 3.4-fold with a yield of 10.0%, and the latter was purified 29-fold with a yield of 15.6%. The two enzymes differ from each other in some enzymic properties such as substrate specificity.
Hosaka
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Department of Applied Chemistry and Biotechnology, Faculty of Engineering Yamanashi University, Japan. g98ds007@ccn.yamanashi.ac.jp
Ui
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Mimura
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D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D000645:Ammonium Sulfate; D001409:Bacillus cereus / Q000201:enzymology*; D005591:Chemical Fractionation; D002848:Chromatography, DEAE-Cellulose; D017886:Durapatite; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D013379:Substrate Specificity
D017886:Durapatite; D000429:Alcohol Oxidoreductases; C118320:acetylacetoin reductase; D000645:Ammonium Sulfate