Reversible immobilization of urease onto Procion Brown MX-5BR-Ni(II) attached polyamide hollow-fibre membranes

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dc.contributor.authorAkgol, S.
dc.contributor.authorYalcinkaya, Y.
dc.contributor.authorBayramoglu, G.
dc.contributor.authorDenizli, A.
dc.contributor.authorArıca, M.Y.
dc.date.accessioned2020-06-25T17:34:55Z
dc.date.available2020-06-25T17:34:55Z
dc.date.issued2002
dc.departmentKırıkkale Üniversitesi
dc.descriptionAkgol, Sinan/0000-0002-8528-1854; AKGOL, Sinan/0000-0003-2836-7181
dc.description.abstractUrease was immobilized onto Procion Brown MX-5BR attached and Ni(II) incorporated microporous polyarnide hollow-fibre membrane via adsorption. Urease immobilization onto the polyamide hollow-fibre membrane from aqueous solutions containing different amounts of urease at different pH was investigated in a batch system. The maximum urease immobilization capacity of the polyamide hollow-fibre membrane was 78 mg g(-1) fibre. The retained adsorbed enzyme activity was found to be 37%. However, the urease adsorption onto the polyamide fibre resulted in a threefold increase in enzyme stability with time at 50 degreesC. The Km values were 18 and 22 mM for the free and the immobilized enzymes, respectively. The V-max values were 59.7 U mg(-1) for the free and 25.9 U mg(-1) for the immobilized enzyme. The optimum pH (7.0) apparently was shifted 1.0 unit acidic region upon immobilization via adsorption. The optimum reaction temperature for the free and the immobilized enzymes were determined to be 45 and 55 degreesC, respectively. The dye-Ni(II) attached polyamide hollow-fibre membranes could be repeatedly used for the adsorption/desorption of enzyme without any significant loss in adsorption capacity. (C) 2002 Elsevier Science Ltd. All rights reserved.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.doi10.1016/S0032-9592(02)00198-X
dc.identifier.endpage683en_US
dc.identifier.issn1359-5113
dc.identifier.issue5en_US
dc.identifier.scopus2-s2.0-0037207018
dc.identifier.scopusqualityQ1
dc.identifier.startpage675en_US
dc.identifier.urihttps://doi.org/10.1016/S0032-9592(02)00198-X
dc.identifier.urihttps://hdl.handle.net/20.500.12587/2953
dc.identifier.volume38en_US
dc.identifier.wosWOS:000179722300006
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.subjectpolyamide hollow-fibre membraneen_US
dc.subjectProcion Brown MX-5BRen_US
dc.subjectadsorptionen_US
dc.subjectenzyme immobilizationen_US
dc.subjectureaseen_US
dc.subjectenzyme reactoren_US
dc.titleReversible immobilization of urease onto Procion Brown MX-5BR-Ni(II) attached polyamide hollow-fibre membranesen_US
dc.typeArticle

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