Dedicated to Professor Karl Hult on the occasion of his 65th birthday.
Review Article
Protein engineering and discovery of lipases†
Article first published online: 25 JAN 2010
DOI: 10.1002/ejlt.200900143
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Issue
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European Journal of Lipid Science and Technology
Special Issue: Oil and fats as renewable resources for the chemical industry
Volume 112, Issue 1, pages 64–74, No. 1 January 2010
Additional Information
How to Cite
Kourist, R., Brundiek, H. and Bornscheuer, U. T. (2010), Protein engineering and discovery of lipases. Eur. J. Lipid Sci. Technol., 112: 64–74. doi: 10.1002/ejlt.200900143
- †
Publication History
- Issue published online: 25 JAN 2010
- Article first published online: 25 JAN 2010
- Manuscript Accepted: 14 SEP 2009
- Manuscript Received: 25 JUN 2009
- Abstract
- References
- Cited By
Keywords:
- Lipase;
- Lipid modification;
- Protein engineering;
- Thermostability
Abstract
Lipases are widely used in the modification of fats and oils with applications in the production of structured triacylglycerols, selective isolation or incorporation of specific fatty acids, and in oleochemistry for the synthesis of emollient esters and sugar fatty acid esters. Despite the numerous examples for the effective use of lipases, the biocatalysts often need to be optimized to show the desired specificities, stability, operational properties, etc. Beside rather classical methods such as variation of the solvent system or carrier for immobilization, the use of protein engineering methods to modify the protein on a molecular level is an important tool for the creation of tailor-designed enzymes. Protein design is also complemented with the efficient isolation of novel lipases from the metagenome. This article covers concepts and examples for the discovery of novel lipases and their variants by protein engineering and metagenome techniques.

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