Coupling Chemical Modification and Immobilization to Improve the Catalytic Performance of Enzymes

Chemical modification and immobilization of enzymes have been usually considered unrelated tools to improve biocatalyst features. However, there are many examples where a chemically modified enzyme is finally used in an immobilized form, and that exemplifies how both tools may be complementary resul...

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Bibliographic Details
Published in:Advanced synthesis & catalysis Vol. 353; no. 13; pp. 2216 - 2238
Main Authors: Rodrigues, Rafael C., Berenguer-Murcia, Ángel, Fernandez-Lafuente, Roberto
Format: Journal Article
Language:English
Published: Weinheim WILEY-VCH Verlag 01-09-2011
WILEY‐VCH Verlag
Wiley-VCH
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Summary:Chemical modification and immobilization of enzymes have been usually considered unrelated tools to improve biocatalyst features. However, there are many examples where a chemically modified enzyme is finally used in an immobilized form, and that exemplifies how both tools may be complementary resulting in a synergism in the final results. In this review we present some of the strategies that may give that result. For example, the chemical modification of soluble enzymes may be used to improve their immobilization (reinforcing adsorption or improving multipoint covalent attachment), or just to improve enzyme stability and facilitate the selection of the immobilization conditions. Chemical modification of previously immobilized enzymes benefits from solid‐phase chemistry due to the nature of enzymes (e.g., prevention of inactivation, aggregation, etc.). The use of different targets for chemical modifications with small molecules or multifunctional polymers are also discussed: intramolecular or intersubunit cross‐linking, one‐point modification, generation of artificial microenvironments, etc.
Bibliography:istex:E82F997EBD4128802AC1736402FF672D6D932CAB
ArticleID:ADSC201100163
ark:/67375/WNG-3BHXJSLS-D
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
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ISSN:1615-4150
1615-4169
1615-4169
DOI:10.1002/adsc.201100163