Immobilization of glucoamylase on the plain and on the spacer arm-attached poly(HEMA-EGDMA) microspheres

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dc.contributor.authorArıca, M.Y.
dc.contributor.authorYavuz, H.
dc.contributor.authorDenizli, A.
dc.date.accessioned2020-06-25T17:34:48Z
dc.date.available2020-06-25T17:34:48Z
dc.date.issued2001
dc.departmentKırıkkale Üniversitesi
dc.description.abstractImmobilization glucoamylase onto plain and a six-carbon spacer arm (i.e., hexamethylene diamine, HMDA) attached poly(2-hydroxyethylmethacrylate-ethylen col dimethacrylate) [poly(HEMA-EGDMA] microspheres was studied. The microspheres were prepared by suspension polymerization and the spacer arm was attached covalently by the reaction of carbonyl groups of poly(HEMA-EGDMA). Glucoamylase was then covalently immobilized either on the plain of microspheres via CNBr activation or on the spacer arm-attached microspheres via CNBr activation and/or using carbodiimide (CDI) as a coupling agent. Incorporation of the spacer arm resulted an increase in the apparent activity of the immobilized enzyme with respect to enzyme immobilized on the plain of the microspheres. The activity yield of the immobilized glucoamylase on the spacer arm-attached poly(HEMA-EGDMA) microspheres was 63% for CDI coupling and 82% for CNBr coupling. This was 44% for the enzyme, which was immobilized on the plain of the unmodified poly(HEMA-EGDMA microspheres via CNBr coupling. The Km values for the immobilized glucoamylase preparations ton the spacer arm-attached microspheres) via CDI coupling 0.9% dextrin (w/v) and CNBr coupling 0.6% dextrin (w/v) were higher than that of the free enzyme 0.2% dextrin (w/v). The temperature profiles were broader for both immobilized preparations than that of the free enzyme. The operational inactivation rate constants (k(iop)) of immobilized enzymes were found to be 1.42 x 10(-5) min(-1) for CNBr coupled and 3.23 x 10(-5) min(-1) for CDI coupled glucoamylase. (C) 2001 John Wiley & Sons, Inc.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.doi10.1002/app.1716
dc.identifier.endpage2710en_US
dc.identifier.issn0021-8995
dc.identifier.issue11en_US
dc.identifier.scopus2-s2.0-0035850611
dc.identifier.scopusqualityQ2
dc.identifier.startpage2702en_US
dc.identifier.urihttps://doi.org/10.1002/app.1716
dc.identifier.urihttps://hdl.handle.net/20.500.12587/2902
dc.identifier.volume81en_US
dc.identifier.wosWOS:000169585100018
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherJohn Wiley & Sons Incen_US
dc.relation.ispartofJournal Of Applied Polymer Science
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectglucoamylaseen_US
dc.subjectenzyme immobilizationen_US
dc.subjectcovalent bondingen_US
dc.subjectspacer armen_US
dc.subjectpoly(HEMA-EGDMA)en_US
dc.subjectmicrospheresen_US
dc.titleImmobilization of glucoamylase on the plain and on the spacer arm-attached poly(HEMA-EGDMA) microspheresen_US
dc.typeArticle

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