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 deposit...

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Bibliographic Details
Published in:Journal of biotechnology 2007-05, Vol.129 (4), p.723-725
Main Authors: Mikolajek, R., Spiess, A.C., Büchs, J.
Format: Article
Language:English
Subjects:
Aldehyde-Lyases - metabolism
Benzaldehydes - chemistry
Benzoin formation
Biodegradation, Environmental
Biological and medical sciences
Biotechnology
Carboligation
Enzymatic catalysis
Enzymes - metabolism
Feasibility Studies
Fundamental and applied biological sciences. Psychology
Gases
Immobilized enzyme
Solid/gas bioreactor
Spectrometry, Fluorescence
Thiamine diphosphate-dependent enzymes
Thiamine Pyrophosphate - metabolism
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Summary: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.
ISSN:0168-1656
1873-4863
DOI:10.1016/j.jbiotec.2007.02.017