Activity of enzymes immobilized in colloidal spherical polyelectrolyte brushes


Dateien zu dieser Ressource

Dateien Größe Format Anzeige

Zu diesem Dokument gibt es keine Dateien.

HAUPT, Björn, Th. NEUMANN, Alexander WITTEMANN, Matthias BALLAUFF, 2005. Activity of enzymes immobilized in colloidal spherical polyelectrolyte brushes. In: Biomacromolecules. 6(2), pp. 948-955. ISSN 1525-7797. Available under: doi: 10.1021/bm0493584

@article{Haupt2005-03Activ-20207, title={Activity of enzymes immobilized in colloidal spherical polyelectrolyte brushes}, year={2005}, doi={10.1021/bm0493584}, number={2}, volume={6}, issn={1525-7797}, journal={Biomacromolecules}, pages={948--955}, author={Haupt, Björn and Neumann, Th. and Wittemann, Alexander and Ballauff, Matthias} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:creator>Haupt, Björn</dc:creator> <dcterms:title>Activity of enzymes immobilized in colloidal spherical polyelectrolyte brushes</dcterms:title> <dcterms:available rdf:datatype="">2012-08-23T08:16:35Z</dcterms:available> <dcterms:isPartOf rdf:resource=""/> <dc:creator>Ballauff, Matthias</dc:creator> <dcterms:issued>2005-03</dcterms:issued> <bibo:uri rdf:resource=""/> <dc:contributor>Ballauff, Matthias</dc:contributor> <dcterms:bibliographicCitation>Publ. in: Biomacromolecules ; 6 (2005), 2. - pp. 948–955</dcterms:bibliographicCitation> <dcterms:abstract xml:lang="eng">We investigate the enzymatic activity of glucoamylase and β-glucosidase adsorbed on a novel type of colloidal particles. The particles used consist of a poly(styrene) core onto which long chains of poly(acrylic acid) or of poly(styrene sulfonic acid) are grafted (“spherical polyelectrolyte brush”). Proteins adsorb spontaneously onto these particles from aqueous solutions if the ionic strength is low. Moreover, the colloidal stability is not impeded by the adsorbed proteins despite the fact that up to 600 mg of enzyme is adsorbed per gram of the carrier particles. The activity of immobilized glucoamylase and β-glucosidase adsorbed onto these particles is analyzed in terms of the Michaelis−Menten parameters. This analysis shows that both enzymes keep nearly their full activity. The Michaelis constant KM differs only slightly from the KM value of the native enzyme when the amount of adsorbed enzyme is raised despite the high local concentration of immobilized enzymes. All data demonstrate that spherical polyelectrolyte brushes present a novel way to immobilize enzymes.</dcterms:abstract> <dc:creator>Neumann, Th.</dc:creator> <dc:date rdf:datatype="">2012-08-23T08:16:35Z</dc:date> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:language>eng</dc:language> <dc:contributor>Neumann, Th.</dc:contributor> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:contributor>Wittemann, Alexander</dc:contributor> <dc:contributor>Haupt, Björn</dc:contributor> <dcterms:rights rdf:resource=""/> <dc:creator>Wittemann, Alexander</dc:creator> <dc:rights>terms-of-use</dc:rights> <dspace:isPartOfCollection rdf:resource=""/> </rdf:Description> </rdf:RDF>

Das Dokument erscheint in:

KOPS Suche


Mein Benutzerkonto