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Purification and properties of acetylacetoin synthase from Bacillus sp. YUF-4.

作者信息

Ui S, Hosaka T, Mizutani K, Mimura A

机构信息

Department of Applied Chemistry & Biotechnology, Faculty of Engineering, Yamanashi University, Japan.

出版信息

Biosci Biotechnol Biochem. 1998 Apr;62(4):795-7. doi: 10.1271/bbb.62.795.

DOI:10.1271/bbb.62.795
PMID:9614712
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.

摘要

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