title: Purification and properties of acetylacetoin synthase from Bacillus sp. YUF-4.
abstract: 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.
authors.affiliation: Department of Applied Chemistry & Biotechnology, Faculty of Engineering, Yamanashi University, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Ui
authors.forename: T
authors.initials: T
authors.lastname: Hosaka
authors.forename: K
authors.initials: K
authors.lastname: Mizutani
authors.forename: A
authors.initials: A
authors.lastname: Mimura
mesh_terms: 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
chemical_list: D000093:Acetoin