ArticleJournal of industrial microbiology & biotechnology2017
A shortened, two-enzyme pathway for 2,3-butanediol production in Escherichia coli.
Article in Journal of industrial microbiology & biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 6 citations in OpenAlex.
- Metabolic Engineering and Regulation of Diol Biosynthesis from Renewable Biomass inBiomolecules · 2022Review
- C4 Bacterial Volatiles Improve Plant Health.Pathogens (Basel, Switzerland) · 2021Review
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
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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