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dc.contributor.authorHudson, Sarah-
dc.contributor.authorCooney, Jakki-
dc.contributor.authorMagner, Edmond-
dc.date.accessioned2011-11-26T07:32:25Z-
dc.date.available2011-11-26T07:32:25Z-
dc.date.issued2008-
dc.identifier.citationAngew. Chem. Int. Ed. 2008, 47, 8582 – 8594en_US
dc.identifier.urihttp://dspace.unimap.edu.my/123456789/16354-
dc.description.abstractMesoporous silicates (MPS) have an ordered pore structure with dimensions comparable to many biological molecules. They have been extensively explored as supports for proteins and enzymes in biocatalytic applications. Since their initial discovery, novel syntheses methods have led to precise control over pore size and structure, particle size, chemical composition, and stability, thus allowing the adsorption of a wide variety of biological macromolecules, such as heme proteins, lipases, antibody fragments, and proteases, into their structures. This Review discusses the application of ordered, largepore, functionalized mesoporous silicates to immobilize proteins for biocatalysis.en_US
dc.language.isoenen_US
dc.publisherWiley-VCH Verlag GmbH & Co. KGaA, Weinheimen_US
dc.subjectBiocatalysisen_US
dc.subjectFunctionalizationen_US
dc.subjectMesoporous materialsen_US
dc.subjectProteinsen_US
dc.subjectSilicatesen_US
dc.titleProteins in Mesoporous Silicatesen_US
dc.typeArticleen_US
dc.identifier.urlwww.angewandte.org-
dc.identifier.doi10.1002/anie.200705238-
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