Literature DB >> 10052142

Separation and properties of two acetylacetoin reductases from Bacillus cereus YUF-4.

T Hosaka1, S Ui, A Mimura.   

Abstract

The separation and purification of two kinds of acetylacetoin reductases (AACRs) from Bacillus cereus YUF-4 were examined. NADPH-linked AACR (AACR I) and NADH-linked AACR (AACR II) were separated from each other by ammonium sulfate fractionation, DEAE-cellulose chromatography, and hydroxyapatite chromatography. The former was purified 3.4-fold with a yield of 10.0%, and the latter was purified 29-fold with a yield of 15.6%. The two enzymes differ from each other in some enzymic properties such as substrate specificity.

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Year:  1999        PMID: 10052142     DOI: 10.1271/bbb.63.199

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  2 in total

1.  Molecular characterization of an NADPH-dependent acetoin reductase/2,3-butanediol dehydrogenase from Clostridium beijerinckii NCIMB 8052.

Authors:  John Raedts; Marco A J Siemerink; Mark Levisson; John van der Oost; Servé W M Kengen
Journal:  Appl Environ Microbiol       Date:  2014-01-17       Impact factor: 4.792

2.  A Green Route for High-Yield Production of Tetramethylpyrazine From Non-Food Raw Materials.

Authors:  Jing Li; Jian Lu; Zhilin Ma; Jianxiu Li; Xianrui Chen; Mengxue Diao; Nengzhong Xie
Journal:  Front Bioeng Biotechnol       Date:  2022-01-25
  2 in total

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