Feasibility of gas/solid carboligation: conversion of benzaldehyde to benzoin using thiamine diphosphate-dependent enzymes.
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.
Mikolajek
R
R
Biochemical Engineering, RWTH Aachen University, Worringer Weg 1, Aachen, Germany.
Spiess
A C
AC
Büchs
J
J
D000446:Aldehyde-Lyases / Q000378:metabolism; D001547:Benzaldehydes / Q000737:chemistry*; D001673:Biodegradation, Environmental; D004798:Enzymes / Q000378:metabolism; D005240:Feasibility Studies; D005740:Gases; D013050:Spectrometry, Fluorescence; D013835:Thiamine Pyrophosphate / Q000378:metabolism*
D001547:Benzaldehydes; D004798:Enzymes; D005740:Gases; D000446:Aldehyde-Lyases; C059416:benzaldehyde lyase; D013835:Thiamine Pyrophosphate; C032175:benzaldehyde