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....
| Main Authors: | , , , , |
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| Other Authors: | , |
| Format: | Article in Journal/Newspaper |
| Language: | unknown |
| Published: |
Elsevier
2004
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| Subjects: | |
| Online Access: | 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 |
| Summary: | 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). |
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