Simultaneous biocatalyst production and Baeyer-Villiger oxidation for bioconversion of cyclohexanone by recombinant Escherichia coli expressing cyclohexanone monooxygenase

Appl Biochem Biotechnol. 2005 Spring:121-124:827-36. doi: 10.1385/abab:123:1-3:0827.

Abstract

Cyclohexanone monooxygenase (CHMO) catalyzing Baeyer-Villiger oxidation converts cyclic ketones into optically pure lactones, which have been used as building blocks in organic synthesis. A recombinant Escherichia coli BL21(DE3)/pMM4 expressing CHMO originated from Acinetobacter sp. NCIB 9871 was used to produce epsilon-caprolactone through a simultaneous biocatalyst production and Baeyer-Villiger oxidation (SPO) process. A fed-batch process was designed to obtain high cell density for improving production of epsilon-caprolactone. The fed-batch SPO process gave the best results, 10.2 g/L of epsilon-caprolactone and 0.34 g/(L.h) of productivity, corresponding to a 10.5- and 3.4-fold enhancement compared with those of the batch SPO, respectively.

Publication types

  • Comparative Study
  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acinetobacter / enzymology*
  • Acinetobacter / genetics
  • Bioreactors / microbiology
  • Biotransformation
  • Caproates / isolation & purification
  • Caproates / metabolism*
  • Catalysis
  • Cell Culture Techniques / methods
  • Cell Proliferation
  • Cyclohexanones / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / growth & development*
  • Escherichia coli / metabolism*
  • Lactones / isolation & purification
  • Lactones / metabolism*
  • Oxidation-Reduction
  • Oxygenases / genetics
  • Oxygenases / metabolism*
  • Protein Engineering / methods*
  • Recombinant Proteins / metabolism

Substances

  • Caproates
  • Cyclohexanones
  • Lactones
  • Recombinant Proteins
  • caprolactone
  • cyclohexanone
  • Oxygenases
  • cyclohexanone oxygenase