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.