Improved biocatalysts by directed evolution and rational protein design

The efficient application of biocatalysts requires the availability of suitable enzymes with high activity and stability under process conditions, desired substrate selectivity and high enantioselectivity. However, wild-type enzymes often need to be optimized to fulfill these requirements. Two rathe...

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Bibliographic Details
Published in:Current Opinion in Chemical Biology 2001-04, Vol.5 (2), p.137-143
Main Authors: Bornscheuer, Uwe T, Pohl, Martina
Format: Article
Language:English
Subjects:
Biocatalysis
Catalysis
directed evolution
Directed Molecular Evolution - methods
Directed Molecular Evolution - trends
Enzyme Activation - physiology
Enzyme Stability - physiology
Enzymes - metabolism
Esterases - genetics
Gene Library
Mutagenesis, Site-Directed - genetics
protein engineering
Protein Engineering - methods
Protein Engineering - trends
Pseudomonas fluorescens - enzymology
rational design
SDM
site-directed mutagenesis
Stereoisomerism
Substrate Specificity - physiology
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Summary:The efficient application of biocatalysts requires the availability of suitable enzymes with high activity and stability under process conditions, desired substrate selectivity and high enantioselectivity. However, wild-type enzymes often need to be optimized to fulfill these requirements. Two rather contradictory tools can be used on a molecular level to create tailor-made biocatalysts: directed evolution and rational protein design.
ISSN:1367-5931
1879-0402
DOI:10.1016/S1367-5931(00)00182-4