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Directed evolution strategies for improved enzymatic performance
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 fur...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2005
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1262762/ https://www.ncbi.nlm.nih.gov/pubmed/16212665 http://dx.doi.org/10.1186/1475-2859-4-29 |
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author | Hibbert, Edward G Dalby, Paul A |
author_facet | Hibbert, Edward G Dalby, Paul A |
author_sort | Hibbert, Edward G |
collection | PubMed |
description | 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. Biocatalysis for organic synthesis frequently makes use of whole-cells, in addition to isolated enzymes, either for a single reaction or for transformations via entire metabolic pathways. As many new whole-cell biocatalysts are being developed by metabolic engineering, the potential of directed evolution to improve these initial designs is also beginning to be realised. |
format | Text |
id | pubmed-1262762 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-12627622005-10-22 Directed evolution strategies for improved enzymatic performance Hibbert, Edward G Dalby, Paul A Microb Cell Fact Review 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. Biocatalysis for organic synthesis frequently makes use of whole-cells, in addition to isolated enzymes, either for a single reaction or for transformations via entire metabolic pathways. As many new whole-cell biocatalysts are being developed by metabolic engineering, the potential of directed evolution to improve these initial designs is also beginning to be realised. BioMed Central 2005-10-07 /pmc/articles/PMC1262762/ /pubmed/16212665 http://dx.doi.org/10.1186/1475-2859-4-29 Text en Copyright © 2005 Hibbert and Dalby; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Hibbert, Edward G Dalby, Paul A Directed evolution strategies for improved enzymatic performance |
title | Directed evolution strategies for improved enzymatic performance |
title_full | Directed evolution strategies for improved enzymatic performance |
title_fullStr | Directed evolution strategies for improved enzymatic performance |
title_full_unstemmed | Directed evolution strategies for improved enzymatic performance |
title_short | Directed evolution strategies for improved enzymatic performance |
title_sort | directed evolution strategies for improved enzymatic performance |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1262762/ https://www.ncbi.nlm.nih.gov/pubmed/16212665 http://dx.doi.org/10.1186/1475-2859-4-29 |
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