Enhanced activity of enzymes immobilized in thermoresponsive core-shell microgels

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WELSCH, Nicole, Alexander WITTEMANN, Matthias BALLAUFF, 2009. Enhanced activity of enzymes immobilized in thermoresponsive core-shell microgels. In: The Journal of Physical Chemistry B. 113(49), pp. 16039-16045. ISSN 1520-6106. eISSN 1520-5207

@article{Welsch2009-12-10Enhan-20189, title={Enhanced activity of enzymes immobilized in thermoresponsive core-shell microgels}, year={2009}, doi={10.1021/jp907508w}, number={49}, volume={113}, issn={1520-6106}, journal={The Journal of Physical Chemistry B}, pages={16039--16045}, author={Welsch, Nicole and Wittemann, Alexander and Ballauff, Matthias} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/20189"> <dc:creator>Ballauff, Matthias</dc:creator> <dc:rights>deposit-license</dc:rights> <dc:creator>Wittemann, Alexander</dc:creator> <dc:contributor>Ballauff, Matthias</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-08-22T09:24:13Z</dc:date> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/20189"/> <dcterms:issued>2009-12-10</dcterms:issued> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-08-22T09:24:13Z</dcterms:available> <dc:contributor>Wittemann, Alexander</dc:contributor> <dc:language>eng</dc:language> <dcterms:title>Enhanced activity of enzymes immobilized in thermoresponsive core-shell microgels</dcterms:title> <dcterms:abstract xml:lang="eng">We present a quantitative study of the catalytic activity of β-d-glucosidase from almonds adsorbed on thermosensitive microgels. The core−shell particles used as a carrier system consist of a solid polystyrene core onto which a poly(N-isopropylacrylamide) (PNiPA) network is grafted. In the swollen state of this microgel, i.e., below the critical solution temperature (LCST) of PNiPA, high amounts of enzyme can be immobilized into the PNiPA network without loss of colloidal stability. The enzymatic activity of β-d-glucosidase in its native form and in the adsorbed state was analyzed in terms of Michaelis−Menten kinetics. Moreover, the dependence of the enzymatic activity on temperature was investigated. We demonstrate that the enzymatic activity of β-d-glucosidase adsorbed on such a core−shell microgel is increased by a factor of more than three compared to its activity in solution. This is in marked contrast to other carrier systems that usually lead to a strong decrease of enzymatic activity. Both the high loading capacity of the carrier observed and the increase of the catalytic activity of immobilized β-d-glucosidase are traced back to the formation of strong interactions between the enzyme and microgel. Studies by Fourier-transform infrared (FT-IR) spectroscopy identify the formation of hydrogen bonds as driving forces for the adsorption. Hydrogen bonding may also be the reason for the enhanced activity.</dcterms:abstract> <dcterms:bibliographicCitation>Publ. in: The Journal of Physical Chemistry B ; 113 (2009), 49. - pp. 16039–16045</dcterms:bibliographicCitation> <dc:creator>Welsch, Nicole</dc:creator> <dc:contributor>Welsch, Nicole</dc:contributor> </rdf:Description> </rdf:RDF>

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