Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures

Autores
Castro, Guillermo Raul; Knubovets, Tatyana
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Biocatalysis in non-aqueous media has undergone tremendous development during the last decade, and numerous reactions have been introduced and optimized for synthetic applications. In contrast to aqueous enzymology, biotransformations in organic solvents offer unique industrially attractive advantages, such as: drastic changes in the enantioselectivity of the reaction, the reversal of the thermodynamic equilibrium of hydrolysis reactions, suppression of water-dependent side reactions, and resistance to bacterial contamination. Currently, the field is dominated by heterogeneous biocatalysis based primarily on lyophilized enzyme powders, cross-linked crystals, and enzymes immobilized on inert supports that are mainly applied in enantioselective synthesis. However, low reaction rates are an inherent problem of the heterogeneous biocatalysis, while the homogeneous systems have the advantage that the elimination of diffusional barriers of substrates and products between organic and water phases results in an increase in the reaction rate. Here the discussion is focused on the correlation between activity and structure of the intact enzymes dissolved in neat organic solvents, as well as modifications of natural enzymes, which make them soluble and catalytically active in non-aqueous environment. Factors that influence conformation and stability of the enzymes are also discussed. Current developments in non-aqueous biocatalysts that combine advantages of protein modification and immobilization, i.e. HIP plastics, enzyme chips, ionic liquids, are characterized. Finally, engineering enzymes for biotransformations in non-conventional media by directed evolution is summarized.
Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Tufts University; Estados Unidos
Fil: Knubovets, Tatyana. Transkariotyc Therapies; Estados Unidos
Materia
Homogeneous Biocatalysis
Organic Solvents
Enzyme Modification
Covalently Modified Enzymes
Coated Enzymes
Enzyme Stability
Reverse Micelles
Hydrophobic Ion Pairing
Directed Evolution
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/42020

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spelling Homogeneous Biocatalysis in Organic Solvents and Water-Organic MixturesCastro, Guillermo RaulKnubovets, TatyanaHomogeneous BiocatalysisOrganic SolventsEnzyme ModificationCovalently Modified EnzymesCoated EnzymesEnzyme StabilityReverse MicellesHydrophobic Ion PairingDirected Evolutionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Biocatalysis in non-aqueous media has undergone tremendous development during the last decade, and numerous reactions have been introduced and optimized for synthetic applications. In contrast to aqueous enzymology, biotransformations in organic solvents offer unique industrially attractive advantages, such as: drastic changes in the enantioselectivity of the reaction, the reversal of the thermodynamic equilibrium of hydrolysis reactions, suppression of water-dependent side reactions, and resistance to bacterial contamination. Currently, the field is dominated by heterogeneous biocatalysis based primarily on lyophilized enzyme powders, cross-linked crystals, and enzymes immobilized on inert supports that are mainly applied in enantioselective synthesis. However, low reaction rates are an inherent problem of the heterogeneous biocatalysis, while the homogeneous systems have the advantage that the elimination of diffusional barriers of substrates and products between organic and water phases results in an increase in the reaction rate. Here the discussion is focused on the correlation between activity and structure of the intact enzymes dissolved in neat organic solvents, as well as modifications of natural enzymes, which make them soluble and catalytically active in non-aqueous environment. Factors that influence conformation and stability of the enzymes are also discussed. Current developments in non-aqueous biocatalysts that combine advantages of protein modification and immobilization, i.e. HIP plastics, enzyme chips, ionic liquids, are characterized. Finally, engineering enzymes for biotransformations in non-conventional media by directed evolution is summarized.Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Tufts University; Estados UnidosFil: Knubovets, Tatyana. Transkariotyc Therapies; Estados UnidosTaylor & Francis2003-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/42020Castro, Guillermo Raul; Knubovets, Tatyana; Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures; Taylor & Francis; Critical Reviews In Biotechnology; 23; 3; 12-2003; 195-2310738-8551CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1080/bty.23.3.195info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.1080/bty.23.3.195info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T10:00:01Zoai:ri.conicet.gov.ar:11336/42020instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-11-12 10:00:02.054CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures
title Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures
spellingShingle Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures
Castro, Guillermo Raul
Homogeneous Biocatalysis
Organic Solvents
Enzyme Modification
Covalently Modified Enzymes
Coated Enzymes
Enzyme Stability
Reverse Micelles
Hydrophobic Ion Pairing
Directed Evolution
title_short Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures
title_full Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures
title_fullStr Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures
title_full_unstemmed Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures
title_sort Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures
dc.creator.none.fl_str_mv Castro, Guillermo Raul
Knubovets, Tatyana
author Castro, Guillermo Raul
author_facet Castro, Guillermo Raul
Knubovets, Tatyana
author_role author
author2 Knubovets, Tatyana
author2_role author
dc.subject.none.fl_str_mv Homogeneous Biocatalysis
Organic Solvents
Enzyme Modification
Covalently Modified Enzymes
Coated Enzymes
Enzyme Stability
Reverse Micelles
Hydrophobic Ion Pairing
Directed Evolution
topic Homogeneous Biocatalysis
Organic Solvents
Enzyme Modification
Covalently Modified Enzymes
Coated Enzymes
Enzyme Stability
Reverse Micelles
Hydrophobic Ion Pairing
Directed Evolution
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Biocatalysis in non-aqueous media has undergone tremendous development during the last decade, and numerous reactions have been introduced and optimized for synthetic applications. In contrast to aqueous enzymology, biotransformations in organic solvents offer unique industrially attractive advantages, such as: drastic changes in the enantioselectivity of the reaction, the reversal of the thermodynamic equilibrium of hydrolysis reactions, suppression of water-dependent side reactions, and resistance to bacterial contamination. Currently, the field is dominated by heterogeneous biocatalysis based primarily on lyophilized enzyme powders, cross-linked crystals, and enzymes immobilized on inert supports that are mainly applied in enantioselective synthesis. However, low reaction rates are an inherent problem of the heterogeneous biocatalysis, while the homogeneous systems have the advantage that the elimination of diffusional barriers of substrates and products between organic and water phases results in an increase in the reaction rate. Here the discussion is focused on the correlation between activity and structure of the intact enzymes dissolved in neat organic solvents, as well as modifications of natural enzymes, which make them soluble and catalytically active in non-aqueous environment. Factors that influence conformation and stability of the enzymes are also discussed. Current developments in non-aqueous biocatalysts that combine advantages of protein modification and immobilization, i.e. HIP plastics, enzyme chips, ionic liquids, are characterized. Finally, engineering enzymes for biotransformations in non-conventional media by directed evolution is summarized.
Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Tufts University; Estados Unidos
Fil: Knubovets, Tatyana. Transkariotyc Therapies; Estados Unidos
description Biocatalysis in non-aqueous media has undergone tremendous development during the last decade, and numerous reactions have been introduced and optimized for synthetic applications. In contrast to aqueous enzymology, biotransformations in organic solvents offer unique industrially attractive advantages, such as: drastic changes in the enantioselectivity of the reaction, the reversal of the thermodynamic equilibrium of hydrolysis reactions, suppression of water-dependent side reactions, and resistance to bacterial contamination. Currently, the field is dominated by heterogeneous biocatalysis based primarily on lyophilized enzyme powders, cross-linked crystals, and enzymes immobilized on inert supports that are mainly applied in enantioselective synthesis. However, low reaction rates are an inherent problem of the heterogeneous biocatalysis, while the homogeneous systems have the advantage that the elimination of diffusional barriers of substrates and products between organic and water phases results in an increase in the reaction rate. Here the discussion is focused on the correlation between activity and structure of the intact enzymes dissolved in neat organic solvents, as well as modifications of natural enzymes, which make them soluble and catalytically active in non-aqueous environment. Factors that influence conformation and stability of the enzymes are also discussed. Current developments in non-aqueous biocatalysts that combine advantages of protein modification and immobilization, i.e. HIP plastics, enzyme chips, ionic liquids, are characterized. Finally, engineering enzymes for biotransformations in non-conventional media by directed evolution is summarized.
publishDate 2003
dc.date.none.fl_str_mv 2003-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/42020
Castro, Guillermo Raul; Knubovets, Tatyana; Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures; Taylor & Francis; Critical Reviews In Biotechnology; 23; 3; 12-2003; 195-231
0738-8551
CONICET Digital
CONICET
url http://hdl.handle.net/11336/42020
identifier_str_mv Castro, Guillermo Raul; Knubovets, Tatyana; Homogeneous Biocatalysis in Organic Solvents and Water-Organic Mixtures; Taylor & Francis; Critical Reviews In Biotechnology; 23; 3; 12-2003; 195-231
0738-8551
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1080/bty.23.3.195
info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.1080/bty.23.3.195
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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