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PEDS Advance Access originally published online on April 19, 2008
Protein Engineering Design and Selection 2008 21(6):387-393; doi:10.1093/protein/gzn014
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© The Author 2008. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Improving activity and stability of cutinase towards the anionic detergent AOT by complete saturation mutagenesis

V. Brissos1,2,4, T. Eggert3, J.M.S. Cabral2,4 and K.-E. Jaeger1

1 Institut für Molekulare Enzymtechnologie, Heinrich-Heine-Universität Düsseldorf, Forschungszentrum Jülich, D-52426 Jülich, Germany 2IBB—Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal 3evocatal GmbH, Merowingerplatz la, D-40225 Düsseldorf, Germany

4 To whom correspondence should be addressed. joaquim.cabral{at}ist.utl.pt (J.M.S.C.); vbrissos{at}itqb.unl.pt (V.B.)

Cutinase is an enzyme suitable for detergent applications as well as for organic synthesis in non-aqueous solvents. However, its inactivation in the presence of anionic surfactants is a problem which we have addressed by creating a complete saturation library. For this, the cutinase gene from Fusarium solani pisi was mutated to incorporate all 19 possible amino acid exchanges at each of the 214 amino acid positions. The resulting library was screened for active variants with improved stability in the presence of the anionic surfactant dioctyl sulfosuccinate sodium salt (AOT). Twenty-four sites in cutinase were discovered where amino acid replacements resulted in a 2–11-fold stability increase as compared to the wild-type enzyme.

Keywords: complete saturation mutagenesis/cutinase/stability/surfactant

Received December 26, 2007; revised February 26, 2008; accepted March 5, 2008.


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