Engineering Acetoin and meso-2,3-Butanediol Biosynthesis in E.coli
Name
23BD Biosynthesis in Ecoli FINAL.pdf
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665.57 KB
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Author(s)
Nielsen, David R.
Yoon, Sang-Hwal
Yuan, Clara J.
Prather, Kristala L. Jones
Alternative Title
Metabolic engineering of acetoin and meso-2, 3-butanediol biosynthesis in E.coli
Date Issued
January 2010
Journal
Biotechnology Journal
Publisher
John Wiley & Sons, Inc.
Citation
Nielsen, David R. et al. “Metabolic engineering of acetoin and meso-2, 3-butanediol biosynthesis in E. coli.” Biotechnology Journal 5.3 (2010): 274-284.
Version
Author's final manuscript
Abstract
The functional reconstruction of acetoin and meso-2,3-butanediol (meso-2,3-BD) biosynthetic
pathways in Escherichia coli have been explored systematically. Pathway construction involved the in vivo screening of prospective pathway isozymes of yeast and bacterial origin. After substantial engineering of the host background to increase pyruvate availability, E. coli YYC202(DE3) ldhA− ilvC− expressing ilvBN from E. coli and aldB from L. lactis (encoding acetolactate synthase and acetolactate decarboxylase activities, respectively) was able to produce up to 870 mg/L acetoin, with no coproduction of diacetyl observed. These strains were also found to produce small quantities of meso-2,3-BD, suggesting the existence of endogenous 2,3-BD dehydrogenase activity. Finally, the coexpression of bdh1 from S. cerevisiae, encoding 2,3-BD dehydrogenase, in this strain resulted in the production of up to 1120 mg/L meso-2,3-BD, with glucose a yield of 0.29 g/g. While disruption of the native lactate biosynthesis pathway increased pyruvate precursor availability to this strain, increased availability of NADH for acetoin reduction to meso-2,3-BD was found to be the most important consequence of ldhA deletion.
MIT Department
Massachusetts Institute of Technology. Department of Chemical Engineering
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Creative Commons Attribution-Noncommercial-Share Alike 3.0
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DOI of Published Version
https://doi.org/10.1002/biot.200900279
