Reversible immobilization of tyrosinase onto polyethyleneimine-grafted and Cu(II) chelated poly(HEMA-co-GMA) reactive membranes

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dc.contributor.authorArica, M.Y.
dc.contributor.authorBayramoglu, G.
dc.date.accessioned2020-06-25T17:40:10Z
dc.date.available2020-06-25T17:40:10Z
dc.date.issued2004
dc.departmentKırıkkale Üniversitesi
dc.description.abstractThe present study describes the preparation of poly(HEMA-co-GMA) reactive membranes that were grafted with polyethylenimine (PEI) following UV photo-polymerization. The immobilization of tyrosinase was carried out via multi-point ionic interactions based on -NH2 groups of PEI and Cu(II) ions. Tyrosinase is a copper-dependent enzyme, which should show a binding affinity for the chelated Cu(II) ions on the membrane surfaces. The tyrosinase immobilization was positively correlated with the input enzyme amount in the immobilization medium. The maximum tyrosinase immobilization capacities of the poly(HEMA-co-GMA)-PEI and poly(HEMA-co-GMA)-PEI-Cu(II) membranes were 19.3 and 24.6 mg/m(2), respectively. The enzyme activity when assessed at various pH and temperatures gave broader range for immobilized preparations when compared to free enzyme. The poly (HEMA-co-GMA)-PEI-Cu(II) tyrosinase membranes retained 82% of their initial activity at the end of 120 h of continuous reaction. Moreover, upon storage for 3 months the activity of the immobilized membranes retained 46% of their initial levels. After deactivation of the enzyme, the poly(HEMA-co-GMA)-PEI membrane was easily regenerated, re-chelated with the Cu(II) ions and reloaded with the enzyme for repeated use. The mild immobilization conditions, easy and rapid membrane preparation, one-step enzyme adsorption at substantially higher levels and membrane reusability are the beneficial properties of such systems and offers promising potential in several biochemical processes. (C) 2003 Elsevier B.V. All rights reserved.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.doi10.1016/j.molcatb.2003.12.006
dc.identifier.endpage265en_US
dc.identifier.issn1381-1177
dc.identifier.issn1873-3158
dc.identifier.issue4-6en_US
dc.identifier.scopus2-s2.0-1242293113
dc.identifier.scopusqualityN/A
dc.identifier.startpage255en_US
dc.identifier.urihttps://doi.org/10.1016/j.molcatb.2003.12.006
dc.identifier.urihttps://hdl.handle.net/20.500.12587/3320
dc.identifier.volume27en_US
dc.identifier.wosWOS:000220344900016
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevieren_US
dc.relation.ispartofJournal Of Molecular Catalysis B-Enzymatic
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectimmobilizationen_US
dc.subjectadsorptionen_US
dc.subjectpolyethylenimineen_US
dc.subjecttyrosinaseen_US
dc.subjecthydrophilic membranesen_US
dc.titleReversible immobilization of tyrosinase onto polyethyleneimine-grafted and Cu(II) chelated poly(HEMA-co-GMA) reactive membranesen_US
dc.typeArticle

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