Proteins in Mesoporous Silicates

dc.contributor.author	Hudson, Sarah
dc.contributor.author	Cooney, Jakki
dc.contributor.author	Magner, Edmond
dc.date.accessioned	2011-11-26T07:32:25Z
dc.date.available	2011-11-26T07:32:25Z
dc.date.issued	2008
dc.identifier.citation	Angew. Chem. Int. Ed. 2008, 47, 8582 – 8594	en_US
dc.identifier.uri	http://dspace.unimap.edu.my/123456789/16354
dc.description.abstract	Mesoporous 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.iso	en	en_US
dc.publisher	Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim	en_US
dc.subject	Biocatalysis	en_US
dc.subject	Functionalization	en_US
dc.subject	Mesoporous materials	en_US
dc.subject	Proteins	en_US
dc.subject	Silicates	en_US
dc.title	Proteins in Mesoporous Silicates	en_US
dc.type	Article	en_US
dc.identifier.url	www.angewandte.org
dc.identifier.doi	10.1002/anie.200705238