Issue 5, 2011
From the journal:

Green Chemistry

Lipase CAL-B does not catalyze a promiscuous decarboxylative aldol addition or Knoevenagel reaction

Andrew S. Evitta  and  Uwe T. Bornscheuer*a  

* Corresponding authors

a Institute of Biochemistry, Dept. of Biotechnology & Enzyme Catalysis, Greifswald University, Felix-Hausdorff-Str. 4, Greifswald, Germany
E-mail: uwe.bornscheuer@uni-greifswald.de
Fax: +49 3834 86 80066
Tel: +49 3834 86 4367

Abstract

Recently it was reported that lipase B from Candida antarctica (CAL-B) shows catalytic promiscuity in the decarboxylative aldol addition and Knoevenagel reaction between 4-nitrobenzaldehyde (4-NBA) and ethyl acetoacetate. We here provide experimental evidence that CAL-B simply catalyzed hydrolysis of the ester yielding the free acetoacetic acid, which under the reaction conditions readily reacts with 4-NBA to the described products.

Graphical abstract: Lipase CAL-B does not catalyze a promiscuous decarboxylative aldol addition or Knoevenagel reaction

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Article information

DOI
https://doi.org/10.1039/C0GC00505C
Article type
Communication
Submitted
01 Sep 2010
Accepted
06 Jan 2011
First published
07 Apr 2011

Green Chem., 2011,13, 1141-1142

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Lipase CAL-B does not catalyze a promiscuous decarboxylative aldol addition or Knoevenagel reaction

A. S. Evitt and U. T. Bornscheuer, Green Chem., 2011, 13, 1141 DOI: 10.1039/C0GC00505C

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