Issue |
OCL
Volume 15, Number 3, Mai-Juin 2008
|
|
---|---|---|
Page(s) | 184 - 188 | |
Section | Dossier | |
DOI | https://doi.org/10.1051/ocl.2008.0192 | |
Published online | 15 May 2008 |
Alteration of lipase properties by protein engineering methods
Department of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487
Greifswald, Germany
+49 3834 86 4367
+49 3834 86 80066
*
uwe.bornscheuer@uni-greifswald.de
Lipases are very important biocatalysts in lipid modification and a broad number of processes have already been established on large scale in industry. A current trend is to tailor-design enzymes for a given application and protein engineering methods are commonly used for this. In this dossier, basic principles of rational protein design and directed evolution are described together with recent examples for the successful application of these tools for the alteration of the substrate specificity, stereoselectivity, and stability of lipases.
Key words: lipase / esterase / protein design / protein engineering / directed evolution / stereoselectivity / stability
© John Libbey Eurotext 2008
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