Biocatalytic production of (2S,3S)-2,3-butanediol from diacetyl using whole cells of engineered Escherichia coli
► We cloned a 2,3-butanediol dehydrogenase gene and expressed it in Escherichia coli. ► We confirmed the stereospecificity of the 2,3-butanediol dehydrogenase. ► We used the engineered E. coli to produce (2S,3S)-2,3-butanediol from diacetyl. ► The concentration of (2S,3S)-2,3-butanediol produced was...
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Published in | Bioresource technology Vol. 115; pp. 111 - 116 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
01.07.2012
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Subjects | |
Online Access | Get full text |
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Summary: | ► We cloned a 2,3-butanediol dehydrogenase gene and expressed it in Escherichia coli. ► We confirmed the stereospecificity of the 2,3-butanediol dehydrogenase. ► We used the engineered E. coli to produce (2S,3S)-2,3-butanediol from diacetyl. ► The concentration of (2S,3S)-2,3-butanediol produced was higher than other reports.
(2S,3S)-2,3-Butanediol ((2S,3S)-2,3-BD) is a crucial chiral compound that acts as an excellent building block in asymmetric synthesis of highly valuable chiral compounds. However, the low concentration and optical purity of (2S,3S)-2,3-BD produced in previous studies limited its applications. In the present work, the gene encoding 2,3-butanediol dehydrogenase from an Enterobacter cloacae ssp. dissolvens strain SDM was cloned and expressed in Escherichia coli. Whole cells of the recombinant E. coli was used to produce (2S,3S)-2,3-BD from diacetyl. Under optimal conditions, high-optical-purity (2S,3S)-2,3-BD (purity >99%) was obtained with concentrations of 16.1gl−1 and 26.8gl−1 in batch and fed-batch conversions, respectively. Thus, the process might be a promising alternative for the production of (2S,3S)-2,3-BD. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0960-8524 1873-2976 |
DOI: | 10.1016/j.biortech.2011.08.097 |