Magnetic polymeric nanospheres as an immobilized metal affinity chromatography (IMAC) support for catalase

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dc.contributor.authorCorman, M. Emin
dc.contributor.authorOzturk, Nevra
dc.contributor.authorTuzmen, Nalan
dc.contributor.authorAkgol, Sinan
dc.contributor.authorDenizli, Adil
dc.date.accessioned2019-10-27T21:18:09Z
dc.date.available2019-10-27T21:18:09Z
dc.date.issued2010
dc.departmentEge Üniversitesien_US
dc.description.abstractNovel magnetic nanospheres with an average size of 118 nm utilizing N-methacryloyl-(L)-cysteine methyl ester (MAC) as a monomer were prepared by surfactant free emulsion polymerization of 2-hydroxyethyl methacrylate (HEMA) and MAC conducted in an aqueous dispersion medium. MAC was synthesized using methacryloyl chloride and L-cysteine methyl ester. L-Cysteine groups of the mag-poly(HEMA-MAC) nanospheres were chelated with Fe3+ ions. Specific surface area of the nonporous nanospheres was found to be 2452 m(2)/g. Mag-poly(HEMA-MAC)-Fe3+ nanospheres contained 0.81 mmol sulphur/g polymer were used in the adsorption of catalase in batch system. Using an optimized adsorption protocol, a very high loading of 820 mg catalase/g nanosphere was obtained. The adsorption phenomena appeared to follow a typical Langmuir isotherm. The immobilized catalase has more resistence to temperature inactivation than that of their free form. The optimum pH value of catalase was not affected by the immobilization reaction, but the pH profile was broadened for the immobilized enzyme. Kinetic parameters were determined for immobilized catalase as well as for the free enzyme. The values of the Michaelis constant K-m of catalase were significantly smaller (ca. 2.5 times) upon immobilization, indicating increased affinity of the enzyme for its substrate, whereas V-max value of free catalase was higher than that of the immobilized enzyme. It was also observed that enzyme could be repeatedly adsorbed and desorbed on the mag-poly(HEMA-MAC)-Fe3+ nanospheres without loss of adsorption capacity or enzymatic activity. (C) 2009 Elsevier B.V. All rights reserved.en_US
dc.identifier.doi10.1016/j.bej.2009.11.002
dc.identifier.endpage164en_US
dc.identifier.issn1369-703X
dc.identifier.issn1873-295X
dc.identifier.issn1369-703Xen_US
dc.identifier.issn1873-295Xen_US
dc.identifier.issue2en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage159en_US
dc.identifier.urihttps://doi.org/10.1016/j.bej.2009.11.002
dc.identifier.urihttps://hdl.handle.net/11454/43932
dc.identifier.volume49en_US
dc.identifier.wosWOS:000276125500002en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.language.isoenen_US
dc.publisherElsevier Science Bven_US
dc.relation.ispartofBiochemical Engineering Journalen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCatalaseen_US
dc.subjectNanospheresen_US
dc.subjectSupporten_US
dc.subjectIMACen_US
dc.subjectCysteineen_US
dc.titleMagnetic polymeric nanospheres as an immobilized metal affinity chromatography (IMAC) support for catalaseen_US
dc.typeArticleen_US

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