Directed evolution strategies for improved enzymatic performance |
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Authors: | Edward?G?Hibbert Email author" target="_blank">Paul?A?DalbyEmail author |
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Institution: | (1) The Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, University College London, Torrington Place, London, WC1E 7JE, UK |
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Abstract: | The engineering of enzymes with altered activity, specificity and stability, using directed evolution techniques that mimic
evolution on a laboratory timescale, is now well established. However, the general acceptance of these methods as a route
to new biocatalysts for organic synthesis requires further improvement of the methods for both ease-of-use and also for obtaining
more significant changes in enzyme properties than is currently possible. Recent advances in library design, and methods of
random mutagenesis, combined with new screening and selection tools, continue to push forward the potential of directed evolution.
For example, protein engineers are now beginning to apply the vast body of knowledge and understanding of protein structure
and function, to the design of focussed directed evolution libraries, with striking results compared to the previously favoured
random mutagenesis and recombination of entire genes. Significant progress in computational design techniques which mimic
the experimental process of library screening is also now enabling searches of much greater regions of sequence-space for
those catalytic reactions that are broadly understood and, therefore, possible to model. |
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Keywords: | |
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