Immobilization of urease via adsorption onto L-histidine-Ni(II) complexed poly(HEMA-MAH) microspheres: Preparation and characterization

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dc.contributor.authorBayramoğlu, Gülay
dc.contributor.authorYalçın, Emin
dc.contributor.authorArıca, M. Yakup
dc.date.accessioned2020-06-25T17:40:20Z
dc.date.available2020-06-25T17:40:20Z
dc.date.issued2005
dc.departmentKırıkkale Üniversitesi
dc.description.abstractPoly(2-hydroxyethyl methacrylate-co-N-methacryloly-L-histidinemethylester) poly(HEMA-MAH) microspheres was prepared via suspension polymerization. L-Histidine groups of the poly(HEMA-MAH) microspheres were then chelated with Ni(II) ions (poly(HEMA-MAH)-Ni(II)). Urease immobilization onto the poly(HEMA-MAH) and poly(HEMA-MAH)-Ni(II) microspheres from aqueous solutions was investigated in a batch system. The amount of immobilized urease on the poly(HEMA-MAH) and poly(REMA-MAH)-Ni(II) was 47.8 and 66.1 mg/g support, respectively. The values of Michaelis constants K-m for both immobilized urease preparations were significant higher than free enzyme, indicating decreased affinity by the enzyme for its substrate, whereas V-max values were smaller for both immobilized urease preparations compared to free enzyme. However, the urease-immobilized onto the poly(HEMA-MAH)-Ni(II) resulted in an increase in enzyme stability with time. Optimum operational temperature for both immobilized preparations was 5.0 degrees C higher than that of the free enzyme and the temperature profiles of the immobilized preparations were significantly broader. It was observed that enzyme could be repeatedly adsorbed and desorbed on the poly(HEMA-MAH) and poly(HEMA-MAH)-Ni(II) microspheres without loss of adsorption capacity or enzymic activity. Finally, a packed bed enzyme-reactor with/urease-immobilized poly(HEMA-MAH)-Ni(II) microspheres, were used for degradation of urea in the continuous operation mode. The enzyme-reactor operated continuously at 35 degrees C for 40 h without significant loss of performance. (c) 2005 Elsevier Ltd. All rights reserved.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.doi10.1016/j.procbio.2005.03.058
dc.identifier.endpage3513en_US
dc.identifier.endpageclosedAccessen_US
dc.identifier.issn1359-5113
dc.identifier.issn1873-3298
dc.identifier.issue11en_US
dc.identifier.scopus2-s2.0-24944483117
dc.identifier.scopusqualityQ1
dc.identifier.startpage3505en_US
dc.identifier.urihttps://doi.org/10.1016/j.procbio.2005.03.058
dc.identifier.urihttps://hdl.handle.net/20.500.12587/3401
dc.identifier.volume40en_US
dc.identifier.wosWOS:000232393700017
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevier Sci Ltden_US
dc.relation.ispartofProcess Biochemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjecturaseen_US
dc.subjectimmobilizationen_US
dc.subjectadsorptionen_US
dc.subjectL-histidineen_US
dc.subjectmicrospheresen_US
dc.titleImmobilization of urease via adsorption onto L-histidine-Ni(II) complexed poly(HEMA-MAH) microspheres: Preparation and characterizationen_US
dc.typeArticle

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