Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.552149
Title: Enzyme immobilisation and catalysis in ordered mesoporous silica
Author: Smith, Graham Murray
Awarding Body: University of St Andrews
Current Institution: University of St Andrews
Date of Award: 2008
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Abstract:
A range of mesoporous materials based on SBA-15 have been prepared and characterised. The materials were templated by neutral block copolymer P123, and typically have a hexagonal (p6mm) pore structure, with high surface areas and narrow pore size distributions. The removal of the surfactant template by calcination and solvent extraction has been investigated. The aqueous stability of this material, and the hydrolysis of the surface was studied. Organic functional groups were incorporated into the silica surface by co-condensation, or by post synthesis grafting. A range of functional groups were incorporated, including amine, carboxy, allyl and thiol groups. The pore size of the materials was controlled by the addition of trimethoxybenzene during synthesis, which significantly increased the pore size and uptake capacity of the materials. The adsorption of CALB by SBA-15 was investigated, with support materials extracted by calcination or solvent extraction. Rapid uptake at high loading was observed, with a maximum loading of 450 mg g-1 measured. The leaching of the enzyme from the support was investigated, and found to be high with unfunctionalised supports. The leaching from functionalised supports incorporating sulfur groups was significantly reduced. The activity of the immobilised CALB was measured by tributyrin hydrolysis in aqueous media, and by enantioselective transesterification of (R)-1-phenylethanol in organic media. The effect of surface functionalisation for reusability and thermal stability in aqueous systems was investigated. Preliminary studies of supported CALB for dynamic kinetic resolution were carried out, with an investigation of acidic zeolites and a mesoporous supported catalyst for 1-phenylethanol racemisation. The encapsulation of immobilised CALB was investigated, and the activity and reusability of these systems studied.
Supervisor: Botting, Nigel P. Sponsor: Avecia Biotechnology
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.552149  DOI: Not available
Keywords: Enzyme ; Mesoporous ; CALB ; Immobilisation ; Hydrolysis ; Transesterification ; SBA-15 ; QP601.S6 ; Immobilized enzymes ; Silica ; Mesoporous materials
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