Design and Evolution of Biocatalysts

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Enzymes as biocatalysts offer several advantages over their chemical counterparts, and as such have attracted much attention for use in the synthesis of various organic compounds. However, despite many successes in the practical application of enzymes, the extensive use of enzymes in the synthesis of organic compounds is still hindered by inadequacy in substrate specificity, catalytic activity, enantio-selectivity and stability. Enzymes with desired functions targeted for practical applications have long been a goal in protein/enzyme engineering. Many approaches have been developed and employed for redesigning enzymes with desired properties, including the structure-guided rational method, directed evolution, computational methods, and combinatorial methods. This review will cover recent advances in the design and evolution of enzymes targeted for specific properties, focusing on the strategy and the applicability of each approach.
Publisher
Bentham Science Publ Ltd
Issue Date
2010-10
Language
English
Article Type
Article
Keywords

SITE-DIRECTED MUTAGENESIS; COMPUTATIONAL PROTEIN DESIGN; CYCLODEXTRIN GLUCANOTRANSFERASE; PHENYLALANINE DEHYDROGENASE; BURKHOLDERIA-GLADIOLI; COENZYME SPECIFICITY; BACILLUS-SPHAERICUS; ESTERASE ESTB; AMINO-ACIDS; ENZYMES

Citation

CURRENT ORGANIC CHEMISTRY, v.14, no.17, pp.1894 - 1901

ISSN
1385-2728
DOI
10.2174/138527210792927609
URI
http://hdl.handle.net/10203/94373
Appears in Collection
BS-Journal Papers(저널논문)
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