Ethanol improves lipase immobilization on a hydrophobic support
A mesoporous silica functionalized with octyl groups had been used as the support for lipase (from Candida antarctica) immobilization. The hydrophobicity provided by the hydrocarbon chains together with the excellent morphologic characteristics of the solid leads to high enzyme loadings in monolayer...
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ftcsic:oai:digital.csic.es:10261/335163 2024-02-11T09:58:31+01:00 Ethanol improves lipase immobilization on a hydrophobic support Blanco Martín, Rosa María Terreros Ceballos, Pilar Muñoz, Núria Serra, Elías M. Ministerio de Educación (España) Comunidad de Madrid 2007-06-01 http://hdl.handle.net/10261/335163 https://doi.org/10.1016/j.molcatb.2007.03.003 https://doi.org/10.13039/100012818 unknown Elsevier http://dx.doi.org/10.1016/j.molcatb.2007.03.003 Sí Journal of Molecular Catalysis - B Enzymatic 47(1-2): 13-20 (2007) 1381-1177 http://hdl.handle.net/10261/335163 doi:10.1016/j.molcatb.2007.03.003 1873-3158 http://dx.doi.org/10.13039/100012818 none Enzyme immobilization Lipase Hydrophobic supports Hydrophobicity Mesoporous silica Monolayer artículo http://purl.org/coar/resource_type/c_6501 2007 ftcsic https://doi.org/10.1016/j.molcatb.2007.03.00310.13039/100012818 2024-01-16T11:52:54Z A mesoporous silica functionalized with octyl groups had been used as the support for lipase (from Candida antarctica) immobilization. The hydrophobicity provided by the hydrocarbon chains together with the excellent morphologic characteristics of the solid leads to high enzyme loadings in monolayer fashion. However, in this kind of systems the aqueous enzyme solution cannot easily access all the inner surface of the pores because of the highly hydrophobic nature of these surfaces. Thus, the presence of low ethanol concentration decreases the hydrophobicity of the channels and the access of enzyme seems to be significantly improved. The monolayer capacity (400–500 mg protein/g of octyl silica) increases twice compared to the corresponding immobilization in the absence of ethanol (200 mg protein/g of octyl silica). The activity of the derivatives prepared in the presence of ethanol was also significantly improved: 33,000 tributyrin units/g of catalyst at the monolayer limit, which is four- to five-fold higher than the activities of the corresponding derivatives prepared in the absence of ethanol. This work was possible thanks to the financial support from Spanish Ministerio de Educacion (project AGL2004-07227-C02-01). Elías Serra acknowledges the support of a Comunidad de Madrid PhD fellowship. Article in Journal/Newspaper Antarc* Antarctica Digital.CSIC (Spanish National Research Council) |
institution |
Open Polar |
collection |
Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
unknown |
topic |
Enzyme immobilization Lipase Hydrophobic supports Hydrophobicity Mesoporous silica Monolayer |
spellingShingle |
Enzyme immobilization Lipase Hydrophobic supports Hydrophobicity Mesoporous silica Monolayer Blanco Martín, Rosa María Terreros Ceballos, Pilar Muñoz, Núria Serra, Elías M. Ethanol improves lipase immobilization on a hydrophobic support |
topic_facet |
Enzyme immobilization Lipase Hydrophobic supports Hydrophobicity Mesoporous silica Monolayer |
description |
A mesoporous silica functionalized with octyl groups had been used as the support for lipase (from Candida antarctica) immobilization. The hydrophobicity provided by the hydrocarbon chains together with the excellent morphologic characteristics of the solid leads to high enzyme loadings in monolayer fashion. However, in this kind of systems the aqueous enzyme solution cannot easily access all the inner surface of the pores because of the highly hydrophobic nature of these surfaces. Thus, the presence of low ethanol concentration decreases the hydrophobicity of the channels and the access of enzyme seems to be significantly improved. The monolayer capacity (400–500 mg protein/g of octyl silica) increases twice compared to the corresponding immobilization in the absence of ethanol (200 mg protein/g of octyl silica). The activity of the derivatives prepared in the presence of ethanol was also significantly improved: 33,000 tributyrin units/g of catalyst at the monolayer limit, which is four- to five-fold higher than the activities of the corresponding derivatives prepared in the absence of ethanol. This work was possible thanks to the financial support from Spanish Ministerio de Educacion (project AGL2004-07227-C02-01). Elías Serra acknowledges the support of a Comunidad de Madrid PhD fellowship. |
author2 |
Ministerio de Educación (España) Comunidad de Madrid |
format |
Article in Journal/Newspaper |
author |
Blanco Martín, Rosa María Terreros Ceballos, Pilar Muñoz, Núria Serra, Elías M. |
author_facet |
Blanco Martín, Rosa María Terreros Ceballos, Pilar Muñoz, Núria Serra, Elías M. |
author_sort |
Blanco Martín, Rosa María |
title |
Ethanol improves lipase immobilization on a hydrophobic support |
title_short |
Ethanol improves lipase immobilization on a hydrophobic support |
title_full |
Ethanol improves lipase immobilization on a hydrophobic support |
title_fullStr |
Ethanol improves lipase immobilization on a hydrophobic support |
title_full_unstemmed |
Ethanol improves lipase immobilization on a hydrophobic support |
title_sort |
ethanol improves lipase immobilization on a hydrophobic support |
publisher |
Elsevier |
publishDate |
2007 |
url |
http://hdl.handle.net/10261/335163 https://doi.org/10.1016/j.molcatb.2007.03.003 https://doi.org/10.13039/100012818 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://dx.doi.org/10.1016/j.molcatb.2007.03.003 Sí Journal of Molecular Catalysis - B Enzymatic 47(1-2): 13-20 (2007) 1381-1177 http://hdl.handle.net/10261/335163 doi:10.1016/j.molcatb.2007.03.003 1873-3158 http://dx.doi.org/10.13039/100012818 |
op_rights |
none |
op_doi |
https://doi.org/10.1016/j.molcatb.2007.03.00310.13039/100012818 |
_version_ |
1790594194341888000 |