Design of epoxy-functionalized Fe3O4@MCM-41 core-shell nanoparticles for enzyme immobilization

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dc.authoridAteş, Burhan/0000-0001-6080-229X
dc.authoridUlu, Ahmet/0000-0002-4447-6233
dc.authoridKoytepe, Suleyman/0000-0002-4788-278X
dc.authorwosidKöytepe, Süleyman/AAA-4168-2021
dc.authorwosidAteş, Burhan/AAA-3730-2021
dc.authorwosidUlu, Ahmet/L-5180-2016
dc.contributor.authorUlu, Ahmet
dc.contributor.authorOzcan, Imren
dc.contributor.authorKoytepe, Suleyman
dc.contributor.authorAtes, Burhan
dc.date.accessioned2024-08-04T20:44:28Z
dc.date.available2024-08-04T20:44:28Z
dc.date.issued2018
dc.departmentİnönü Üniversitesien_US
dc.description.abstractThe scope of our research was to prepare the organosilane-modified Fe3O4@MCM-41 core-shell magnetic nano particles, used for L-ASNase immobilization and explored screening of immobilization conditions such as pH, temperature, thermal stability, kinetic parameters, reusability and storage stability. In this content, Fe3O4 core shell magnetic nanoparticles were prepared via co-precipitation method and coated with MCM-41. Then, Fe3O4@MCM-41 magnetic nanoparticles were functionalized by (3-glycidyloxypropyl) trimethoxysilane (GPTMS) as an organosilane compound. Subsequently, L-ASNase was covalently immobilized on epoxyfunctionalized Fe3O4@MCM-41 magnetic nanoparticles. The immobilized L-ASNase had greater activity at high pH and temperature values. It also maintained >92% of the initial activity after incubation at 55 degrees C for 3 h. Regarding kinetic values, immobilized L-ASNase showed a higher Vmax and lower Km compared to native L-ASNase. In addition, it displayed excellent reusability for 12 successive cycles. After 30 days of storage at 4 degrees C and 25 degrees C, immobilized L-ASNase retained 54% and 26% of its initial activities while native L-ASNase lost about 68% and 84% of its initial activity, respectively. As a result, the immobilization of L-ASNase onto magnetic nanoparticles may provide an advantage in terms of removal of L-ASNase from reaction media. (C) 2018 Elsevier B.V. All rights reserved.en_US
dc.description.sponsorshipInonu University Research Councilen_US
dc.description.sponsorshipWe are thankful to the Inonu University Research Council for partial support of this work.en_US
dc.identifier.doi10.1016/j.ijbiomac.2018.04.157
dc.identifier.endpage1130en_US
dc.identifier.issn0141-8130
dc.identifier.issn1879-0003
dc.identifier.pmid29727644en_US
dc.identifier.scopus2-s2.0-85046644502en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage1122en_US
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2018.04.157
dc.identifier.urihttps://hdl.handle.net/11616/98273
dc.identifier.volume115en_US
dc.identifier.wosWOS:000438662500127en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relation.ispartofInternational Journal of Biological Macromoleculesen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectEpoxy-functionalizeden_US
dc.subjectFe3O4@MCM-41en_US
dc.subjectCore-shell nanoparticlesen_US
dc.subjectL-Asparaginaseen_US
dc.subjectEnzyme immobilizationen_US
dc.titleDesign of epoxy-functionalized Fe3O4@MCM-41 core-shell nanoparticles for enzyme immobilizationen_US
dc.typeArticleen_US

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