Vanillin production using Escherichia coli cells over-expressing isoeugenol monooxygenase of Pseudomonas putida

Biotechnol Lett. 2008 Apr;30(4):665-70. doi: 10.1007/s10529-007-9602-4. Epub 2007 Nov 27.

Abstract

The isoeugenol monooxygenase gene of Pseudomonas putida IE27 was inserted into an expression vector, pET21a, under the control of the T7 promoter. The recombinant plasmid was introduced into Escherichia coli BL21(DE3) cells, containing no vanillin-degrading activity. The transformed E. coli BL21(DE3) cells produced 28.3 g vanillin/l from 230 mM isoeugenol, with a molar conversion yield of 81% at 20 degrees C after 6 h. In the reaction system, no accumulation of undesired by-products, such as vanillic acid or acetaldehyde, was observed.

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Benzaldehydes / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Eugenol / analogs & derivatives*
  • Eugenol / chemistry
  • Eugenol / metabolism
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / metabolism*
  • Molecular Structure
  • Pseudomonas putida / enzymology*
  • Pseudomonas putida / genetics

Substances

  • Bacterial Proteins
  • Benzaldehydes
  • Eugenol
  • isoeugenol
  • vanillin
  • Mixed Function Oxygenases