Directed evolution of enzymes for applied biocatalysis.
Directed evolution has rapidly emerged as a powerful new strategy for improving the characteristics of enzymes in a targeted manner. By coupling various protocols for generating large variant libraries of genes, together with high-throughput screens that select for specific properties of an enzyme, such as thermostability, catalytic activity and substrate specificity, it is now possible to optimize biocatalysts for specific applications. However, further work is required to broaden the range of screens that can be used, particularly in terms of reaction type, such as hydroxylation and carbon-carbon bond formation, and functional characteristics, such as enantioselectivity and regioselectivity, so that directed evolution can be used in a routine manner for biocatalyst development.
Turner
Nicholas J
NJ
School of Chemistry, University of Edinburgh, King's Buildings, West Mains Road, Edinburgh EH9 3JJ, Scotland, UK. n.j.turner@ed.ac.uk
D001709:Biotechnology; D002384:Catalysis; D019020:Directed Molecular Evolution / Q000379:methods; D004795:Enzyme Stability; D004798:Enzymes / Q000235:genetics* / Q000378:metabolism*; D005821:Genetic Techniques; D016296:Mutagenesis; D015202:Protein Engineering / Q000379:methods; D013237:Stereoisomerism; D013379:Substrate Specificity / Q000235:genetics
D004798:Enzymes