Purification and properties of acetylacetoin synthase from Bacillus sp. YUF-4.
In Bacillus sp. YUF-4, acetylacetoin synthase was induced by acetoin, while glucose inhibited the induction. The enzyme was purified 111-fold by 6 purification steps, and a further purification followed, by HPLC using a TSK gel, Phenyl-5PW RP. The resulting enzyme gave a single band with a molecular mass of 62 kDa by SDS-PAGE and 220 kDa by gel filtration. Some enzymic characteristics were studied.
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Department of Applied Chemistry & Biotechnology, Faculty of Engineering, Yamanashi University, Japan.
Hosaka
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Mizutani
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Mimura
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D000093:Acetoin / Q000494:pharmacology; D001407:Bacillus / Q000187:drug effects / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight
D000093:Acetoin