Chemical Modification in the Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities
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http://hdl.handle.net/10045/65891
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Campo DC | Valor | Idioma |
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dc.contributor | Materiales Carbonosos y Medio Ambiente | es_ES |
dc.contributor.author | Rueda, Nazzoly | - |
dc.contributor.author | Santos, Jose Cleiton S. dos | - |
dc.contributor.author | Ortiz, Claudia | - |
dc.contributor.author | Torres, Rodrigo | - |
dc.contributor.author | Barbosa, Oveimar | - |
dc.contributor.author | Rodrigues, Rafael C. | - |
dc.contributor.author | Berenguer-Murcia, Ángel | - |
dc.contributor.author | Fernández Lafuente, Roberto | - |
dc.contributor.other | Universidad de Alicante. Departamento de Química Inorgánica | es_ES |
dc.contributor.other | Universidad de Alicante. Instituto Universitario de Materiales | es_ES |
dc.date.accessioned | 2017-05-11T10:35:18Z | - |
dc.date.available | 2017-05-11T10:35:18Z | - |
dc.date.issued | 2016-06 | - |
dc.identifier.citation | The Chemical Record. 2016, 16(3): 1436-1455. doi:10.1002/tcr.201600007 | es_ES |
dc.identifier.issn | 1527-8999 (Print) | - |
dc.identifier.issn | 1528-0691 (Online) | - |
dc.identifier.uri | http://hdl.handle.net/10045/65891 | - |
dc.description.abstract | Chemical modification of enzymes and immobilization used to be considered as separate ways to improve enzyme properties. This review shows how the coupled use of both tools may greatly improve the final biocatalyst performance. Chemical modification of a previously immobilized enzyme is far simpler and easier to control than the modification of the free enzyme. Moreover, if protein modification is performed to improve its immobilization (enriching the enzyme in reactive groups), the final features of the immobilized enzyme may be greatly improved. Chemical modification may be directed to improve enzyme stability, but also to improve selectivity, specificity, activity, and even cell penetrability. Coupling of immobilization and chemical modification with site-directed mutagenesis is a powerful instrument to obtain fully controlled modification. Some new ideas such as photoreceptive enzyme modifiers that change their physical properties under UV exposition are discussed. | es_ES |
dc.description.sponsorship | This work has been supported by grant CTQ2013-41507-R from Spanish MINECO, grant no. 1102-489-25428 from COLCIENCIAS, the Universidad Industrial de Santander (VIE-UIS Research Program, Colombia), and CNPq grant 403505/2013-5 (Brazil). A.B.-M. thanks the Spanish MINECO for a Ramon y Cajal fellowship (RyC-2009-03813). Predoctoral fellowships for N.R. (Colciencias, Colombian Government) and J.C.S.d.S. (CNPq, Brazil) are also recognized. | es_ES |
dc.language | eng | es_ES |
dc.publisher | Wiley-VCH Verlag GmbH & Co. KGaA | es_ES |
dc.rights | © 2016 The Chemical Society of Japan & Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim | es_ES |
dc.subject | Enzymes | es_ES |
dc.subject | Polymers | es_ES |
dc.subject | Photochemistry | es_ES |
dc.subject | Structure–activity relationships | es_ES |
dc.subject | Supported catalysts | es_ES |
dc.subject.other | Química Inorgánica | es_ES |
dc.title | Chemical Modification in the Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.peerreviewed | si | es_ES |
dc.identifier.doi | 10.1002/tcr.201600007 | - |
dc.relation.publisherversion | http://dx.doi.org/10.1002/tcr.201600007 | es_ES |
dc.rights.accessRights | info:eu-repo/semantics/restrictedAccess | es_ES |
Aparece en las colecciones: | INV - MCMA - Artículos de Revistas |
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