Functionalization of mesoporous silica for lipase immobilization: Characterization of the support and the catalysts
A support for enzyme immobilization was prepared by functionalization of mesoporous silica with octyltriethoxysilane. The features of the surface enables the adsorption of lipase from Candida antarctica B via strong hydrophobic interactions, enhancing the stability of the adsorbed enzyme molecules....
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ftcsic:oai:digital.csic.es:10261/335171 2024-02-11T09:58:40+01:00 Functionalization of mesoporous silica for lipase immobilization: Characterization of the support and the catalysts Blanco Martín, Rosa María Terreros Ceballos, Pilar Fernández-Pérez, Mónica Otero Hernández, Cristina Dı́az-González, Guadalupe Comisión Interministerial de Ciencia y Tecnología, CICYT (España) Comunidad de Madrid 2004-08-03 http://hdl.handle.net/10261/335171 https://doi.org/10.1016/j.molcatb.2004.03.012 https://doi.org/10.13039/501100007273 https://doi.org/10.13039/100012818 unknown Elsevier http://dx.doi.org/10.1016/j.molcatb.2004.03.012 Sí Journal of Molecular Catalysis - B Enzymatic 30(2): 83-93 (2004) 1381-1177 http://hdl.handle.net/10261/335171 doi:10.1016/j.molcatb.2004.03.012 1873-3158 http://dx.doi.org/10.13039/501100007273 http://dx.doi.org/10.13039/100012818 none Lipase Immobilization Silica Adsorption Ethanolamine Candida antarctica B artículo http://purl.org/coar/resource_type/c_6501 2004 ftcsic https://doi.org/10.1016/j.molcatb.2004.03.01210.13039/50110000727310.13039/100012818 2024-01-16T11:52:54Z A support for enzyme immobilization was prepared by functionalization of mesoporous silica with octyltriethoxysilane. The features of the surface enables the adsorption of lipase from Candida antarctica B via strong hydrophobic interactions, enhancing the stability of the adsorbed enzyme molecules. Derivatives with a high enzyme loading (200 mg protein/g of silica) can be obtained due to the high porosity and surface properties of the support while the immobilization occurs in a monolayer fashion. The lack of inactive enzyme aggregates, together with the high enzyme loading, are responsible for the high catalytic activity achieved by these species. Derivatives were prepared with different lipase loading, and the activities were tested and compared to the commercial derivative Novozym 435. The stability of the catalyst and hence its industrial applicability were tested by performing subsequent reaction cycles of acylation of ethanolamine with lauric acid in acetonitrile. Conversion was quantitative even after 15 reaction cycles. Financial support of this work was obtained from the project number PPQ2000-1329 (Spanish CICYT), and the fellowship for Monica Fernandez-Perez (Comunidad de Madrid). Article in Journal/Newspaper Antarc* Antarctica Digital.CSIC (Spanish National Research Council) Fernandez ENVELOPE(-62.233,-62.233,-63.250,-63.250) Perez ENVELOPE(-69.117,-69.117,-68.517,-68.517) |
institution |
Open Polar |
collection |
Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
unknown |
topic |
Lipase Immobilization Silica Adsorption Ethanolamine Candida antarctica B |
spellingShingle |
Lipase Immobilization Silica Adsorption Ethanolamine Candida antarctica B Blanco Martín, Rosa María Terreros Ceballos, Pilar Fernández-Pérez, Mónica Otero Hernández, Cristina Dı́az-González, Guadalupe Functionalization of mesoporous silica for lipase immobilization: Characterization of the support and the catalysts |
topic_facet |
Lipase Immobilization Silica Adsorption Ethanolamine Candida antarctica B |
description |
A support for enzyme immobilization was prepared by functionalization of mesoporous silica with octyltriethoxysilane. The features of the surface enables the adsorption of lipase from Candida antarctica B via strong hydrophobic interactions, enhancing the stability of the adsorbed enzyme molecules. Derivatives with a high enzyme loading (200 mg protein/g of silica) can be obtained due to the high porosity and surface properties of the support while the immobilization occurs in a monolayer fashion. The lack of inactive enzyme aggregates, together with the high enzyme loading, are responsible for the high catalytic activity achieved by these species. Derivatives were prepared with different lipase loading, and the activities were tested and compared to the commercial derivative Novozym 435. The stability of the catalyst and hence its industrial applicability were tested by performing subsequent reaction cycles of acylation of ethanolamine with lauric acid in acetonitrile. Conversion was quantitative even after 15 reaction cycles. Financial support of this work was obtained from the project number PPQ2000-1329 (Spanish CICYT), and the fellowship for Monica Fernandez-Perez (Comunidad de Madrid). |
author2 |
Comisión Interministerial de Ciencia y Tecnología, CICYT (España) Comunidad de Madrid |
format |
Article in Journal/Newspaper |
author |
Blanco Martín, Rosa María Terreros Ceballos, Pilar Fernández-Pérez, Mónica Otero Hernández, Cristina Dı́az-González, Guadalupe |
author_facet |
Blanco Martín, Rosa María Terreros Ceballos, Pilar Fernández-Pérez, Mónica Otero Hernández, Cristina Dı́az-González, Guadalupe |
author_sort |
Blanco Martín, Rosa María |
title |
Functionalization of mesoporous silica for lipase immobilization: Characterization of the support and the catalysts |
title_short |
Functionalization of mesoporous silica for lipase immobilization: Characterization of the support and the catalysts |
title_full |
Functionalization of mesoporous silica for lipase immobilization: Characterization of the support and the catalysts |
title_fullStr |
Functionalization of mesoporous silica for lipase immobilization: Characterization of the support and the catalysts |
title_full_unstemmed |
Functionalization of mesoporous silica for lipase immobilization: Characterization of the support and the catalysts |
title_sort |
functionalization of mesoporous silica for lipase immobilization: characterization of the support and the catalysts |
publisher |
Elsevier |
publishDate |
2004 |
url |
http://hdl.handle.net/10261/335171 https://doi.org/10.1016/j.molcatb.2004.03.012 https://doi.org/10.13039/501100007273 https://doi.org/10.13039/100012818 |
long_lat |
ENVELOPE(-62.233,-62.233,-63.250,-63.250) ENVELOPE(-69.117,-69.117,-68.517,-68.517) |
geographic |
Fernandez Perez |
geographic_facet |
Fernandez Perez |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://dx.doi.org/10.1016/j.molcatb.2004.03.012 Sí Journal of Molecular Catalysis - B Enzymatic 30(2): 83-93 (2004) 1381-1177 http://hdl.handle.net/10261/335171 doi:10.1016/j.molcatb.2004.03.012 1873-3158 http://dx.doi.org/10.13039/501100007273 http://dx.doi.org/10.13039/100012818 |
op_rights |
none |
op_doi |
https://doi.org/10.1016/j.molcatb.2004.03.01210.13039/50110000727310.13039/100012818 |
_version_ |
1790594385831788544 |