Hybrid composites octyl-silica-methacrylate agglomerates as enzyme supports
The use of immobilized enzymes as catalysts may be limited by particle size which must be larger than the mesh that retains them in the reactor. Octyl-silica (OS) beads of 70 μm average size were agglomerated to obtain hybrid organic–inorganic composites with particle sizes between 100 and 200 μm. The agglomeration process has been achieved by polymerization of methacrylate from glycidyl methacrylate and ethylene dimethacrylate in the presence of silica beads and further functionalization of the composite with octyl groups. Methacrylate content of the composite (20%) is high enough to stick OS beads, and low enough to preserve the advantages of these particles as supports. The properties of the octyl silica particles for lipase immobilization have been very closely reproduced with the octyl-silica-methacrylate (OSM) composite. Enzyme loading of 210 mg lipase per gram of support has been achieved on OSM vs 230 mg/g on OS. Also catalytic activity values are close for both catalysts, OSM-lipase remaining fully active and stable after 15 cycles in acetonitrile.
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Elsevier
2013
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Subjects: | Diffusional limitations, Hybrid composites, Hydrophobic supports, Particle agglomeration, Enzyme immobilization, |
Online Access: | http://hdl.handle.net/10261/100046 http://dx.doi.org/10.13039/501100006280 |
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dig-cial-es-10261-1000462018-09-18T12:13:18Z Hybrid composites octyl-silica-methacrylate agglomerates as enzyme supports Fernández, Óscar Díaz Carretero, Isabel Torres, Carlos F. Tobajas, Montserrat Tejedor, Víctor Blanco Martín, Rosa María Ministerio de Ciencia y Tecnología (España) Diffusional limitations Hybrid composites Hydrophobic supports Particle agglomeration Enzyme immobilization The use of immobilized enzymes as catalysts may be limited by particle size which must be larger than the mesh that retains them in the reactor. Octyl-silica (OS) beads of 70 μm average size were agglomerated to obtain hybrid organic–inorganic composites with particle sizes between 100 and 200 μm. The agglomeration process has been achieved by polymerization of methacrylate from glycidyl methacrylate and ethylene dimethacrylate in the presence of silica beads and further functionalization of the composite with octyl groups. Methacrylate content of the composite (20%) is high enough to stick OS beads, and low enough to preserve the advantages of these particles as supports. The properties of the octyl silica particles for lipase immobilization have been very closely reproduced with the octyl-silica-methacrylate (OSM) composite. Enzyme loading of 210 mg lipase per gram of support has been achieved on OSM vs 230 mg/g on OS. Also catalytic activity values are close for both catalysts, OSM-lipase remaining fully active and stable after 15 cycles in acetonitrile. This work has been supported by the Spanish project MAT-2009-13569. Peer Reviewed 2014-07-17T08:00:11Z 2014-07-17T08:00:11Z 2013 2014-07-17T08:00:12Z artículo http://purl.org/coar/resource_type/c_6501 doi: 10.1016/j.apcata.2012.10.021 issn: 0926-860X Applied Catalysis A: General 450: 204-210 (2013) http://hdl.handle.net/10261/100046 10.1016/j.apcata.2012.10.021 http://dx.doi.org/10.13039/501100006280 none Elsevier |
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Diffusional limitations Hybrid composites Hydrophobic supports Particle agglomeration Enzyme immobilization Diffusional limitations Hybrid composites Hydrophobic supports Particle agglomeration Enzyme immobilization |
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Diffusional limitations Hybrid composites Hydrophobic supports Particle agglomeration Enzyme immobilization Diffusional limitations Hybrid composites Hydrophobic supports Particle agglomeration Enzyme immobilization Fernández, Óscar Díaz Carretero, Isabel Torres, Carlos F. Tobajas, Montserrat Tejedor, Víctor Blanco Martín, Rosa María Hybrid composites octyl-silica-methacrylate agglomerates as enzyme supports |
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The use of immobilized enzymes as catalysts may be limited by particle size which must be larger than the mesh that retains them in the reactor. Octyl-silica (OS) beads of 70 μm average size were agglomerated to obtain hybrid organic–inorganic composites with particle sizes between 100 and 200 μm. The agglomeration process has been achieved by polymerization of methacrylate from glycidyl methacrylate and ethylene dimethacrylate in the presence of silica beads and further functionalization of the composite with octyl groups. Methacrylate content of the composite (20%) is high enough to stick OS beads, and low enough to preserve the advantages of these particles as supports. The properties of the octyl silica particles for lipase immobilization have been very closely reproduced with the octyl-silica-methacrylate (OSM) composite. Enzyme loading of 210 mg lipase per gram of support has been achieved on OSM vs 230 mg/g on OS. Also catalytic activity values are close for both catalysts, OSM-lipase remaining fully active and stable after 15 cycles in acetonitrile. |
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Ministerio de Ciencia y Tecnología (España) |
author_facet |
Ministerio de Ciencia y Tecnología (España) Fernández, Óscar Díaz Carretero, Isabel Torres, Carlos F. Tobajas, Montserrat Tejedor, Víctor Blanco Martín, Rosa María |
format |
artículo |
topic_facet |
Diffusional limitations Hybrid composites Hydrophobic supports Particle agglomeration Enzyme immobilization |
author |
Fernández, Óscar Díaz Carretero, Isabel Torres, Carlos F. Tobajas, Montserrat Tejedor, Víctor Blanco Martín, Rosa María |
author_sort |
Fernández, Óscar |
title |
Hybrid composites octyl-silica-methacrylate agglomerates as enzyme supports |
title_short |
Hybrid composites octyl-silica-methacrylate agglomerates as enzyme supports |
title_full |
Hybrid composites octyl-silica-methacrylate agglomerates as enzyme supports |
title_fullStr |
Hybrid composites octyl-silica-methacrylate agglomerates as enzyme supports |
title_full_unstemmed |
Hybrid composites octyl-silica-methacrylate agglomerates as enzyme supports |
title_sort |
hybrid composites octyl-silica-methacrylate agglomerates as enzyme supports |
publisher |
Elsevier |
publishDate |
2013 |
url |
http://hdl.handle.net/10261/100046 http://dx.doi.org/10.13039/501100006280 |
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