Immobilization of lipase B within micron-sized poly-N-isopropylacrylamide hydrogel particles by solvent exchange
dc.contributor.author | Gawlitza, Kornelia | |
dc.contributor.author | Wu, Changzhu | |
dc.contributor.author | Georgieva, Radostina | |
dc.contributor.author | Wang, Dayang | |
dc.contributor.author | Ansorge-Schumacher, Marion B. | |
dc.contributor.author | Klitzing, Regine von | |
dc.date.accessioned | 2016-06-28T06:13:31Z | |
dc.date.available | 2016-06-28T06:13:31Z | |
dc.date.issued | 2012 | |
dc.description | Dieser Beitrag ist mit Zustimmung des Rechteinhabers aufgrund einer (DFG geförderten) Allianz- bzw. Nationallizenz frei zugänglich. | de |
dc.description | This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively. | en |
dc.description.abstract | The aim of the present work is the use of a water soluble enzyme in an organic solvent, still with a pronounced catalytic activity. Therefore, lipase B from Candida antarctica (CalB) is immobilized within micron-sized thermosensitive p-NIPAM hydrogel particles using a solvent exchange from polar to organic solvents. The absorbed amount of CalB is investigated at different immobilization temperatures. Confocal laser scanning microscopy (CLSM) shows that CalB is homogeneously distributed within the polymer network. An enhanced specific activity of CalB in n-hexane is achieved after immobilization within the p-NIPAM microgels. In order to get information on the supply of the substrate depending on the temperature, the activity is determined at different reaction temperatures. Additionally, the system is stable in the organic solvent, namely n-hexane, and shows a good reusability. | en |
dc.description.sponsorship | DFG, EXC 314, Unifying Concepts in Catalysis | en |
dc.identifier.eissn | 1463-9076 | |
dc.identifier.pmid | 22684227 | |
dc.identifier.uri | https://depositonce.tu-berlin.de/handle/11303/5693 | |
dc.identifier.uri | http://dx.doi.org/10.14279/depositonce-5313 | |
dc.language.iso | en | |
dc.rights.uri | http://rightsstatements.org/vocab/InC/1.0/ | en |
dc.subject.ddc | 540 Chemie und zugeordnete Wissenschaften | de |
dc.title | Immobilization of lipase B within micron-sized poly-N-isopropylacrylamide hydrogel particles by solvent exchange | en |
dc.type | Article | en |
dc.type.version | publishedVersion | en |
dcterms.bibliographicCitation.doi | 10.1039/c2cp40624a | |
dcterms.bibliographicCitation.issue | 27 | |
dcterms.bibliographicCitation.journaltitle | Physical chemistry, chemical physics | en |
dcterms.bibliographicCitation.originalpublishername | Royal Society of Chemistry | de |
dcterms.bibliographicCitation.originalpublisherplace | Cambridge | de |
dcterms.bibliographicCitation.pageend | 9600 | |
dcterms.bibliographicCitation.pagestart | 9594 | |
dcterms.bibliographicCitation.volume | 14 | |
tub.accessrights.dnb | domain | |
tub.affiliation | Fak. 2 Mathematik und Naturwissenschaften::Inst. Chemie | de |
tub.affiliation.faculty | Fak. 2 Mathematik und Naturwissenschaften | de |
tub.affiliation.institute | Inst. Chemie | de |
tub.publisher.universityorinstitution | Technische Universität Berlin |
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