Covalent immobilization of chloroperoxidase onto magnetic beads: Catalytic properties and stability

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dc.contributor.authorBayramoglu, Guelay
dc.contributor.authorKiralp, Senem
dc.contributor.authorYilmaz, Meltem
dc.contributor.authorToppare, Levent
dc.contributor.authorArica, M. Yakup
dc.date.accessioned2020-06-25T17:48:00Z
dc.date.available2020-06-25T17:48:00Z
dc.date.issued2008
dc.description.abstractAmino groups containing magnetic beads were used in covalent immobilization of the enzyme "chloroperoxidase (CPO)" which is one of a few enzymes that can catalyse the peroxide dependent oxidation of a wide spectrum of organic and inorganic compounds. The magnetic poly(glycidylmethacrylate-methylmethacrylate-etbyleneglycol dimethacrylate), magnetic p(GMA-MMA-EGDMA) beads were prepared via suspension polymerization in the presence of ferric ions. The magnetic beads were characterized with scanning electron microscope (SEM), Fourier transform infrared (FTIR), Mossbauer spectroscopy and vibrating sample magnetometer (VSM). The magnetic beads were derivatized sequentially with ammonia and glutaraldehyde, and CPO was covalently immobilized on the support via reaction of the amino groups of the enzyme under mild conditions. The effect of various parameters including pH, temperature and enzyme concentration on the immobilization efficiency of CPO onto glutaric dialdhyde activated magnetic beads was evaluated. Magnetic measurement revealed that the resultant CPO-immobilized magnetic beads were superparamagnetic with a saturation magnetization of 18.2 emu/g. The analysis of FTIR spectra confirmed the binding of CPO on the magnetic beads. The maximum amount of immobilized CPO on the magnetic beads was 2.94 mg/g support. The values of Michaelis constants Km for immobilized CPO was significantly larger, indicating decreased affinity by the enzyme for its substrate, whereas V-max values were smaller for the immobilized CPO. However, the CPO immobilized on the magnetic beads resulted in an increase in enzyme stability with time. (c) 2007 Elsevier B.V. All rights reserved.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.doi10.1016/j.bej.2007.06.018
dc.identifier.endpage188en_US
dc.identifier.issn1369-703X
dc.identifier.issn1873-295X
dc.identifier.issue2en_US
dc.identifier.scopus2-s2.0-37348998909
dc.identifier.scopusqualityQ2
dc.identifier.startpage180en_US
dc.identifier.urihttps://doi.org10.1016/j.bej.2007.06.018
dc.identifier.urihttps://hdl.handle.net/20.500.12587/4224
dc.identifier.volume38en_US
dc.identifier.wosWOS:000252915700007
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevieren_US
dc.relation.ispartofBiochemical Engineering Journal
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectmagnetic beadsen_US
dc.subjectenzyme immobilizationen_US
dc.subjectchloroperoxidaseen_US
dc.subjectkinetic parametersen_US
dc.subjectenzyme stabilityen_US
dc.titleCovalent immobilization of chloroperoxidase onto magnetic beads: Catalytic properties and stabilityen_US
dc.typeArticle

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