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A shortened, two-enzyme pathway for 2,3-butanediol production in Escherichia coli
The platform chemical 2,3-butanediol (2,3-BDO) is produced by a number of microorganisms via a three-enzyme pathway starting from pyruvate. Here, we report production of 2,3-BDO via a shortened, two-enzyme pathway in Escherichia coli . A synthetic operon consisting of the acetolactate synthase (ALS)...
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Published in: | Journal of industrial microbiology & biotechnology 2017-09, Vol.44 (9), p.1273-1277 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The platform chemical 2,3-butanediol (2,3-BDO) is produced by a number of microorganisms via a three-enzyme pathway starting from pyruvate. Here, we report production of 2,3-BDO via a shortened, two-enzyme pathway in
Escherichia coli
. A synthetic operon consisting of the acetolactate synthase (ALS) and acetoin reductase (AR) genes from
Enterobacter
under control of the T7 promoter was cloned in an episomal plasmid.
E. coli
transformed with this plasmid produced 2,3-BDO and the pathway intermediate acetoin, demonstrating that the shortened pathway was functional. To assemble a synthetic operon for inducer- and plasmid-free production of 2,3-BDO, ALS and AR genes were integrated in the
E. coli
genome under control of the constitutive
ackA
promoter. Shake flask-level cultivation led to accumulation of ~1 g/L acetoin and ~0.66 g/L 2,3-BDO in the medium. The novel biosynthetic route for 2,3-BDO biosynthesis described herein provides a simple and cost-effective approach for production of this important chemical. |
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ISSN: | 1367-5435 1476-5535 |
DOI: | 10.1007/s10295-017-1957-5 |