Comparative study of catalase immobilization via adsorption on P(MMA-co-PEG500MA) structures as an effective polymer support

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dc.authoridUlu, Ahmet/0000-0002-4447-6233
dc.authoridAteş, Burhan/0000-0001-6080-229X
dc.authoridKoytepe, Suleyman/0000-0002-4788-278X
dc.authorwosidUlu, Ahmet/L-5180-2016
dc.authorwosidAteş, Burhan/AAA-3730-2021
dc.authorwosidKöytepe, Süleyman/AAA-4168-2021
dc.contributor.authorSel, Evren
dc.contributor.authorUlu, Ahmet
dc.contributor.authorAtes, Burhan
dc.contributor.authorKoytepe, Suleyman
dc.date.accessioned2024-08-04T20:47:22Z
dc.date.available2024-08-04T20:47:22Z
dc.date.issued2021
dc.departmentİnönü Üniversitesien_US
dc.description.abstractIn this study, poly[methyl methacrylate-co-poly(ethylene glycol) methacrylate] (P(MMA-co-PEG500MA)) copolymers were used for catalase (CAT) immobilization. Firstly, P(MMA-co-PEG500MA) copolymers were synthesized by using different amount of methyl methacrylate (MMA) and poly(ethylene glycol) methacrylate (PEG500MA) monomers. The synthesized copolymers were characterized by different analysis techniques. Afterward, CAT enzyme was immobilized via physical adsorption method onto the P(MMA-co-PEG500MA) copolymers. P3 sample containing 1:1 (PEG500MA:MMA) monomer molar ratio was selected as model support because of exhibiting optimum surface porosity and thermal stability. A high immobilization yield (76%) was achieved under optimized conditions. The immobilized enzyme displayed improved tolerance towards pH and temperature changes. After immobilization, the optimum pH shifted from 7.5 to 7.0, whereas the optimum temperature remained unchanged at 35 degrees C. Immobilized enzyme showed good reuse potential and excellent storage stability. After 10 consecutive uses, immobilized enzyme maintained about 51.0% of its initial activity. Furthermore, free enzyme completely lost its initial activity after 4 weeks, while immobilized enzyme maintained approximately 65% of the initial activity at 25 degrees C. Approximately twofold decrease in Km was obtained which means that the affinity of enzyme to the substrate improved after immobilization. Finally, it can be concluded that the prepared P(MMA-co-PEG500MA) copolymer structure can be an ideal matrix for CAT immobilization.en_US
dc.identifier.doi10.1007/s00289-020-03233-0
dc.identifier.endpage2684en_US
dc.identifier.issn0170-0839
dc.identifier.issn1436-2449
dc.identifier.issue5en_US
dc.identifier.scopus2-s2.0-85085298882en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage2663en_US
dc.identifier.urihttps://doi.org/10.1007/s00289-020-03233-0
dc.identifier.urihttps://hdl.handle.net/11616/99307
dc.identifier.volume78en_US
dc.identifier.wosWOS:000535160600001en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofPolymer Bulletinen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectEnzyme immobilizationen_US
dc.subjectCatalaseen_US
dc.subjectCopolymeren_US
dc.subjectReusabilityen_US
dc.titleComparative study of catalase immobilization via adsorption on P(MMA-co-PEG500MA) structures as an effective polymer supporten_US
dc.typeArticleen_US

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