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Article: Enzyme immobilization on amino-functionalized mesostructured cellular foam surfaces, characterization and catalytic properties

TitleEnzyme immobilization on amino-functionalized mesostructured cellular foam surfaces, characterization and catalytic properties
Authors
KeywordsCatalytic Activity
Enzyme Immobilisation
Enzyme Stability
Functionalized Mesoporous Materials
Glucose Oxidase
Issue Date2005
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/molcatb
Citation
Journal Of Molecular Catalysis B: Enzymatic, 2005, v. 33 n. 1-2, p. 43-50 How to Cite?
AbstractLarge mesopores cellular foam (LMCFs) materials with diameters ranging from 17 to 34 nm were synthesized using microemulsion templating. The amine functional groups were attached to channels of LMCFs materials via post-synthesis grafting. The structural and chemical properties of these prepared materials were characterized by TEM, XRD, FTIR and nitrogen adsorption. The glucose oxidase (GOx) was immobilized by covalently couple enzyme molecules to the interior surface of amino-functionalized mesostructured cellular foams (AF-MCFs) materials, in which leaching of the enzyme is prevented. The immobilized enzyme exhibited the high catalytic activity and thermal stability for oxidation of glucose. It was found that GOx immobilized on AF-MCFs materials is re-useable. © 2005 Published by Elsevier B.V.
Persistent Identifierhttp://hdl.handle.net/10722/167914
ISSN
2016 Impact Factor: 2.269
2020 SCImago Journal Rankings: 0.324
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Xen_US
dc.contributor.authorGuan, RFen_US
dc.contributor.authorWu, DQen_US
dc.contributor.authorChan, KYen_US
dc.date.accessioned2012-10-08T03:12:53Z-
dc.date.available2012-10-08T03:12:53Z-
dc.date.issued2005en_US
dc.identifier.citationJournal Of Molecular Catalysis B: Enzymatic, 2005, v. 33 n. 1-2, p. 43-50en_US
dc.identifier.issn1381-1177en_US
dc.identifier.urihttp://hdl.handle.net/10722/167914-
dc.description.abstractLarge mesopores cellular foam (LMCFs) materials with diameters ranging from 17 to 34 nm were synthesized using microemulsion templating. The amine functional groups were attached to channels of LMCFs materials via post-synthesis grafting. The structural and chemical properties of these prepared materials were characterized by TEM, XRD, FTIR and nitrogen adsorption. The glucose oxidase (GOx) was immobilized by covalently couple enzyme molecules to the interior surface of amino-functionalized mesostructured cellular foams (AF-MCFs) materials, in which leaching of the enzyme is prevented. The immobilized enzyme exhibited the high catalytic activity and thermal stability for oxidation of glucose. It was found that GOx immobilized on AF-MCFs materials is re-useable. © 2005 Published by Elsevier B.V.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/molcatben_US
dc.relation.ispartofJournal of Molecular Catalysis B: Enzymaticen_US
dc.subjectCatalytic Activityen_US
dc.subjectEnzyme Immobilisationen_US
dc.subjectEnzyme Stabilityen_US
dc.subjectFunctionalized Mesoporous Materialsen_US
dc.subjectGlucose Oxidaseen_US
dc.titleEnzyme immobilization on amino-functionalized mesostructured cellular foam surfaces, characterization and catalytic propertiesen_US
dc.typeArticleen_US
dc.identifier.emailChan, KY:hrsccky@hku.hken_US
dc.identifier.authorityChan, KY=rp00662en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.molcatb.2005.02.001en_US
dc.identifier.scopuseid_2-s2.0-17844399524en_US
dc.identifier.hkuros116501-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-17844399524&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume33en_US
dc.identifier.issue1-2en_US
dc.identifier.spage43en_US
dc.identifier.epage50en_US
dc.identifier.isiWOS:000229394200007-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridZhang, X=7410265236en_US
dc.identifier.scopusauthoridGuan, RF=8357457500en_US
dc.identifier.scopusauthoridWu, DQ=36767267500en_US
dc.identifier.scopusauthoridChan, KY=7406034142en_US
dc.identifier.issnl1381-1177-

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