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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Published in: | Advanced synthesis & catalysis Vol. 353; no. 13; pp. 2216 - 2238 |
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Main Authors: | , , |
Format: | Journal Article |
Language: | English |
Published: |
Weinheim
WILEY-VCH Verlag
01-09-2011
WILEY‐VCH Verlag Wiley-VCH |
Subjects: | |
Online Access: | Get full text |
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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. |
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Bibliography: | istex:E82F997EBD4128802AC1736402FF672D6D932CAB ArticleID:ADSC201100163 ark:/67375/WNG-3BHXJSLS-D ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 1615-4150 1615-4169 1615-4169 |
DOI: | 10.1002/adsc.201100163 |