Identification and characterization of a short-chain acyl dehydrogenase from Klebsiella pneumoniae and its application for high-level production of L-2,3-butanediol

J Ind Microbiol Biotechnol. 2014 Sep;41(9):1425-33. doi: 10.1007/s10295-014-1483-7. Epub 2014 Jul 19.

Abstract

Klebsiella pneumoniae synthesize large amounts of L-2,3-butanediol (L-2,3-BD), but the underlying mechanism has been unknown. In this study, we provide the first identification and characterization of an L-2,3-BD dehydrogenase from K. pneumoniae, demonstrating its reductive activities toward diacetyl and acetoin, and oxidative activity toward L-2,3-BD. Optimum pH, temperature, and kinetics determined for reductive and oxidative reactions support the preferential production of 2,3-BD during cell growth. Synthesis of L-2,3-BD was remarkably enhanced by increasing gene dosage, reaching levels that, to the best of our knowledge, are the highest achieved to date.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetoin / metabolism
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Butylene Glycols / metabolism*
  • Butyryl-CoA Dehydrogenase / chemistry*
  • Butyryl-CoA Dehydrogenase / genetics
  • Butyryl-CoA Dehydrogenase / metabolism*
  • Enzyme Stability
  • Klebsiella pneumoniae / chemistry
  • Klebsiella pneumoniae / enzymology*
  • Klebsiella pneumoniae / genetics
  • Klebsiella pneumoniae / metabolism
  • Molecular Sequence Data
  • Sequence Alignment

Substances

  • Bacterial Proteins
  • Butylene Glycols
  • 2,3-butylene glycol
  • Acetoin
  • Butyryl-CoA Dehydrogenase