A facile immobilization of polyphenol oxidase enzyme on graphene oxide and reduced graphene oxide thin films: An insight into in-vitro activity measurements and characterization

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dc.contributor.authorGur, Bahri
dc.contributor.authorAyhan, Muhammed Emre
dc.contributor.authorTurkhan, Ayse
dc.contributor.authorGur, Fatma
dc.contributor.authorKaya, Elif Duygu
dc.date.accessioned2024-02-23T14:02:31Z
dc.date.available2024-02-23T14:02:31Z
dc.date.issued2019
dc.departmentNEÜen_US
dc.description.abstractGraphene oxide (GO) and reduced graphene oxide (rGO) Langmuir-Blodgett (LB) films with specific surface properties and functional groups were prepared as negative ideal substrates. Immobilization of the polyphenol oxidase (PPO) enzyme on these films was easily accomplished by electrostatic interaction without the need for any chemical bonding or surface modification. The PPO binding regions to GO and rGO surfaces were shown by an electrostatic surface potential map for pH: 5.0 value. The catalytic performances of the enzyme immobilized on GO and rGO substrates were found to be higher in GO-PPO LB films compared to RGO-PPO LB films in-vitro media. The reason why in-vitro enzyme activity is higher in GO-PPO LB films than in rGO-PPO LB films was also proved by SEM studies. The immobilization onto both the GO and rGO thin films as the GO-PPO and rGO-PPO complexes were further demonstrated by FT-IR measurement. This study revealed that the immobilized PPO enzyme on biodegradable GO is superior to the inorganic materials in terms of its use in biological systems. In addition, the fact that regular film structures with a single molecule thickness were prepared by LB film technique, contributed to the stability and recycling of immobilization of PPO enzyme on GO and rGO. In this respect, the in-vitro storage stability of immobilization on both film structures was determined to be one month at + 4 degrees C.en_US
dc.identifier.doi10.1016/j.colsurfa.2018.11.041
dc.identifier.endpage185en_US
dc.identifier.issn0927-7757
dc.identifier.issn1873-4359
dc.identifier.scopus2-s2.0-85056907904en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage179en_US
dc.identifier.urihttps://doi.org/10.1016/j.colsurfa.2018.11.041
dc.identifier.urihttps://hdl.handle.net/20.500.12452/11746
dc.identifier.volume562en_US
dc.identifier.wosWOS:000454428500022en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherElsevier Science Bven_US
dc.relation.ispartofColloids And Surfaces A-Physicochemical And Engineering Aspectsen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCatalytic Performanceen_US
dc.subjectElectrostatic Surface Potentialen_US
dc.subjectLangmuir-Blodgetten_US
dc.subjectPolyphenol Oxidaseen_US
dc.titleA facile immobilization of polyphenol oxidase enzyme on graphene oxide and reduced graphene oxide thin films: An insight into in-vitro activity measurements and characterizationen_US
dc.typeArticleen_US

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