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Mesoporous Silicas with Tunable Morphology for the Immobilization of Laccase

Siliceous ordered mesoporous materials (OMM) are gaining interest as supports for enzyme immobilization due to their uniform pore size, large surface area, tunable pore network and the introduction of organic components to mesoporous structure. We used SBA-15 type silica materials, which exhibit a r...

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Autores principales: Gascón, Victoria, Díaz, Isabel, Márquez-Álvarez, Carlos, Blanco, Rosa M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6272017/
https://www.ncbi.nlm.nih.gov/pubmed/24886935
http://dx.doi.org/10.3390/molecules19067057
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author Gascón, Victoria
Díaz, Isabel
Márquez-Álvarez, Carlos
Blanco, Rosa M.
author_facet Gascón, Victoria
Díaz, Isabel
Márquez-Álvarez, Carlos
Blanco, Rosa M.
author_sort Gascón, Victoria
collection PubMed
description Siliceous ordered mesoporous materials (OMM) are gaining interest as supports for enzyme immobilization due to their uniform pore size, large surface area, tunable pore network and the introduction of organic components to mesoporous structure. We used SBA-15 type silica materials, which exhibit a regular 2D hexagonal packing of cylindrical mesopores of uniform size, for non-covalent immobilization of laccase. Synthesis conditions were adjusted in order to obtain supports with different particle shape, where those with shorter channels had higher loading capacity. Despite the similar isoelectric points of silica and laccase and the close match between the size of laccase and the pore dimensions of these SBA-15 materials, immobilization was achieved with very low leaching. Surface modification of macro-/mesoporous amorphous silica by grafting of amine moieties was proved to significantly increase the isoelectric point of this support and improve the immobilization yield.
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spelling pubmed-62720172018-12-21 Mesoporous Silicas with Tunable Morphology for the Immobilization of Laccase Gascón, Victoria Díaz, Isabel Márquez-Álvarez, Carlos Blanco, Rosa M. Molecules Article Siliceous ordered mesoporous materials (OMM) are gaining interest as supports for enzyme immobilization due to their uniform pore size, large surface area, tunable pore network and the introduction of organic components to mesoporous structure. We used SBA-15 type silica materials, which exhibit a regular 2D hexagonal packing of cylindrical mesopores of uniform size, for non-covalent immobilization of laccase. Synthesis conditions were adjusted in order to obtain supports with different particle shape, where those with shorter channels had higher loading capacity. Despite the similar isoelectric points of silica and laccase and the close match between the size of laccase and the pore dimensions of these SBA-15 materials, immobilization was achieved with very low leaching. Surface modification of macro-/mesoporous amorphous silica by grafting of amine moieties was proved to significantly increase the isoelectric point of this support and improve the immobilization yield. MDPI 2014-05-30 /pmc/articles/PMC6272017/ /pubmed/24886935 http://dx.doi.org/10.3390/molecules19067057 Text en © 2014 by the authors. licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Gascón, Victoria
Díaz, Isabel
Márquez-Álvarez, Carlos
Blanco, Rosa M.
Mesoporous Silicas with Tunable Morphology for the Immobilization of Laccase
title Mesoporous Silicas with Tunable Morphology for the Immobilization of Laccase
title_full Mesoporous Silicas with Tunable Morphology for the Immobilization of Laccase
title_fullStr Mesoporous Silicas with Tunable Morphology for the Immobilization of Laccase
title_full_unstemmed Mesoporous Silicas with Tunable Morphology for the Immobilization of Laccase
title_short Mesoporous Silicas with Tunable Morphology for the Immobilization of Laccase
title_sort mesoporous silicas with tunable morphology for the immobilization of laccase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6272017/
https://www.ncbi.nlm.nih.gov/pubmed/24886935
http://dx.doi.org/10.3390/molecules19067057
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