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Purification and properties of acetylacetoin synthase from Bacillus sp. YUF-4
1Department of Applied Chemistry & Biotechnology, Faculty of Engineering, Yamanashi University, Japan.
Bioscience, Biotechnology, and Biochemistry
|June 6, 1998
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.