Feasibility of gas/solid carboligation: conversion of benzaldehyde to benzoin using thiamine diphosphate-dependent enzymes

J Biotechnol. 2007 May 10;129(4):723-5. doi: 10.1016/j.jbiotec.2007.02.017. Epub 2007 Feb 27.

Abstract

A carboligation was investigated for the first time as an enzymatic gas phase reaction, where benzaldehyde was converted to benzoin using thiamine diphosphate (ThDP)-dependent enzymes, namely benzaldehyde lyase (BAL) and benzoylformate decarboxylase (BFD). The biocatalyst was immobilized per deposition on non-porous support. Some limitations of the gas/solid biocatalysis are discussed based on this carboligation and it is also demonstrated that the solid/gas system is an interesting tool for more volatile products.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehyde-Lyases / metabolism
  • Benzaldehydes / chemistry*
  • Biodegradation, Environmental*
  • Enzymes / metabolism
  • Feasibility Studies
  • Gases
  • Spectrometry, Fluorescence
  • Thiamine Pyrophosphate / metabolism*

Substances

  • Benzaldehydes
  • Enzymes
  • Gases
  • Aldehyde-Lyases
  • benzaldehyde lyase
  • Thiamine Pyrophosphate
  • benzaldehyde