Synthesis of cinnamyl alcohol from cinnamaldehyde with Bacillus stearothermophilus alcohol dehydrogenase as the isolated enzyme and in recombinant E. coli cells

Appl Biochem Biotechnol. 2013 Jul;170(6):1482-90. doi: 10.1007/s12010-013-0282-3. Epub 2013 May 19.

Abstract

The synthesis of the aroma chemical cinnamyl alcohol (CMO) by means of enzymatic reduction of cinnamaldehyde (CMA) was investigated using NADH-dependent alcohol dehydrogenase from Bacillus stearothermophilus both as an isolated enzyme, and in recombinant Escherichia coli whole cells. The influence of parameters such as reaction time and cofactor, substrate, co-substrate 2-propanol and biocatalyst concentrations on the bioreduction reaction was investigated and an efficient and sustainable one-phase system developed. The reduction of CMA (0.5 g/L, 3.8 mmol/L) by the isolated enzyme occurred in 3 h at 50 °C with 97% conversion, and yielded high purity CMO (≥98%) with a yield of 88% and a productivity of 50 g/genzyme. The reduction of 12.5 g/L (94 mmol/L) CMA by whole cells in 6 h, at 37 °C and no requirement of external cofactor occurred with 97% conversion, 82% yield of 98% pure alcohol and a productivity of 34 mg/gwet cell weight. The results demonstrate the microbial system as a practical and efficient method for larger-scale synthesis of CMO.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acrolein / analogs & derivatives*
  • Acrolein / chemistry
  • Acrolein / metabolism
  • Alcohol Dehydrogenase / chemistry*
  • Alcohol Dehydrogenase / metabolism*
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Geobacillus stearothermophilus / enzymology*
  • Geobacillus stearothermophilus / genetics
  • Propanols / chemical synthesis*
  • Propanols / metabolism*
  • Recombinant Proteins / metabolism

Substances

  • Propanols
  • Recombinant Proteins
  • Acrolein
  • Alcohol Dehydrogenase
  • cinnamaldehyde
  • cinnamyl alcohol