Effect of sol-gel encapsulation on lipase structure and function: a small angle neutron scattering study

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dc.contributor.authorRodgers, LEen_AU
dc.contributor.authorHolden, PJen_AU
dc.contributor.authorKnott, RBen_AU
dc.contributor.authorFinnie, KSen_AU
dc.contributor.authorBartlett, JRen_AU
dc.contributor.authorFoster, LJRen_AU
dc.date.accessioned2009-11-17T01:14:57Zen_AU
dc.date.accessioned2010-04-30T05:06:38Zen_AU
dc.date.available2009-11-17T01:14:57Zen_AU
dc.date.available2010-04-30T05:06:38Zen_AU
dc.date.issued2005-01en_AU
dc.date.statistics2005-01en_AU
dc.description.abstractThe application of small angle neutron scattering (SANS) to the characterisation of sol–gel hosts containing biomolecules offers the opportunity to explore the relationship between gel structure and catalyst. A model system involving the immobilisation of Candida antarctica lipase B (CALB) was investigated. Gels were produced by fluoride-catalysed hydrolysis of fixed ratios of tetramethylorthosilicate (TMOS) and methyltrimethoxysilane (MTMS). Phase separation between the enzyme and the evolving sol–gel matrix was minimised by incorporating glycerol into the sol–gel precursor solution. The potential stabilising effect of the NaF catalyst upon the enzyme was also investigated. Scattering studies were conducted on both immobilised lipase, and lipase in free solution. Scattering studies on free enzyme provided evidence of multiple populations of enzyme aggregates and showed that choice of solvent affected the degree of aggregation. Both NaF and glycerol affected neutron scattering, indicating changes in lipase conformation. Increasing glycerol concentration increased the degree of aggregation and produced differences in solvent packing on the surface of protein molecules. Initial evidence from SANS data indicated that the presence of the enzyme during gel formation conferred structural changes on the gel matrix. Modelling the effect of sol–gel encapsulation on lipase requires comparison of data from free enzyme to the immobilised form. Removal of the enzyme from the sol–gel structure, post gelation, is necessary to better characterise the modified matrix. This methodological problem will be the subject of future investigations. © 2005, Springer.en_AU
dc.identifier.citationRodgers, L. E., Holden, P. J., Knott, R. B., Finnie, K. S., Bartlett, J. R., & Foster, L. J. R. (2005). Effect of sol-gel encapsulation on lipase structure and function: a small angle neutron scattering study. Journal of Sol-Gel Science and Technology, 33(1), 65-69. doi:10.1007/s10971-005-6701-3en_AU
dc.identifier.govdoc1426en_AU
dc.identifier.issn0928-0707en_AU
dc.identifier.journaltitleJournal of Sol-Gel Science and Technologyen_AU
dc.identifier.pagination65-69en_AU
dc.identifier.urihttp://dx.doi.org/10.1007/s10971-005-6701-3en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/2331en_AU
dc.identifier.volume1en_AU
dc.language.isoenen_AU
dc.publisherSpringeren_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectLipasesen_AU
dc.subjectCandidaen_AU
dc.subjectSol-gel processen_AU
dc.subjectGlycerolen_AU
dc.subjectEnzymesen_AU
dc.titleEffect of sol-gel encapsulation on lipase structure and function: a small angle neutron scattering studyen_AU
dc.typeJournal Articleen_AU
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