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Metabolic engineering of acetoin and meso-2, 3-butanediol biosynthesis in E. coli

  1. David R. Nielsen1,2,
  2. Sang-Hwal Yoon1,
  3. Clara J. Yuan1,
  4. Kristala L. J. Prather Professor1,*

Article first published online: 8 MAR 2010

DOI: 10.1002/biot.200900279

Issue

Biotechnology Journal

Biotechnology Journal

Special Issue: Focus: Microbial Biotech

Volume 5, Issue 3, pages 274–284, March 2010

Additional Information

How to Cite

Nielsen, D. R., Yoon, S.-H., Yuan, C. J. and Prather, K. L. J. (2010), Metabolic engineering of acetoin and meso-2, 3-butanediol biosynthesis in E. coli. Biotechnology Journal, 5: 274–284. doi: 10.1002/biot.200900279

Author Information

  1. 1

    Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA

  2. 2

    Chemical Engineering, Arizona State University, Tempe, AZ 85287-6106, USA

*Department of Chemical Engineering, Massachusetts Institute of Technology, Room 66-458, Cambridge, MA 02139, USA, Fax: +1-617-258-5042

Publication History

  1. Issue published online: 8 MAR 2010
  2. Article first published online: 8 MAR 2010
  3. Manuscript Accepted: 13 JAN 2010
  4. Manuscript Revised: 31 DEC 2009
  5. Manuscript Received: 9 DEC 2009

Funded by

  • Natural Sciences and Engineering Research Council of Canada
  • Korean Government – Korea Research Foundation Grant

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Keywords:

  • 2,3-Butanediol;
  • Acetoin;
  • Escherichia coli;
  • Metabolic engineering;
  • NADH

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 vsivo 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.

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