Preparation and characterization of amino and carboxyl functionalized core-shell Fe3O4/SiO2 for L-asparaginase immobilization: A comparison study

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dc.authoridAteş, Burhan/0000-0001-6080-229X
dc.authoridUlu, Ahmet/0000-0002-4447-6233;
dc.authorwosidNOMA, SAMIR/ABH-1773-2021
dc.authorwosidAteş, Burhan/AAA-3730-2021
dc.authorwosidUlu, Ahmet/L-5180-2016
dc.authorwosidKöytepe, Süleyman/AAA-4168-2021
dc.contributor.authorNoma, Samir Abbas Ali
dc.contributor.authorUlu, Ahmet
dc.contributor.authorKoytepe, Suleyman
dc.contributor.authorAtes, Burhan
dc.date.accessioned2024-08-04T20:47:22Z
dc.date.available2024-08-04T20:47:22Z
dc.date.issued2020
dc.departmentİnönü Üniversitesien_US
dc.description.abstractMagnetic nanoparticles are well known as facile and effective support for enzyme immobilization since they have a high surface area, large surface-to-volume ratio, easy separation, a fast and high enzyme loading. This study aims to provide insights on whether acidic or basic modified particles are more effective for L-asparaginase (ASNase) immobilization. Therefore, amino (Fe3O4/SiO2/NH2) and carboxyl-functionalized (Fe3O4/SiO2/COOH) particles were prepared. The functional groups, crystalline structure, magnetic properties, morphology, chemical composition and thermal behaviour of the prepared modified nanoparticles were examined via Fourier-transform infra-red spectroscopy (FTIR), X-ray diffraction (XRD), vibrating-sample magnetometer (VSM), scanning electron microscopy (SEM) and energy-dispersive X-ray spectroscopy (EDAX). Under the optimum conditions, the immobilized enzymes were more stable within a certain range of temperatures and pH values in comparison to free enzyme. On the other hand, the immobilized enzymes showed greater stability after incubation for 3 h at 50 degrees C. The free enzyme maintained only 30% of its initial activity for 4 weeks at 4 degrees C, while Fe3O4/SiO2/NH2/ASNase and Fe3O4/SiO2/COOH/ASNase retained more than 78.9% and 56.5% of initial activities under the same conditions, respectively. Moreover, Fe3O4/SiO2/NH2/ASNase (77.2%) and Fe3O4/SiO2/COOH/ASNase (57.4%) displayed excellent operational stability after 17 repeated cycles. These findings suggested that the Fe3O4/SiO2/NH2 and Fe3O4/SiO2/COOH may be utilized as efficient and sustainable supports to developed immobilized ASNase in several biotechnological applications.en_US
dc.identifier.doi10.1080/10242422.2020.1767605
dc.identifier.endpage404en_US
dc.identifier.issn1024-2422
dc.identifier.issn1029-2446
dc.identifier.issue5en_US
dc.identifier.scopus2-s2.0-85085518430en_US
dc.identifier.scopusqualityQ3en_US
dc.identifier.startpage392en_US
dc.identifier.urihttps://doi.org/10.1080/10242422.2020.1767605
dc.identifier.urihttps://hdl.handle.net/11616/99311
dc.identifier.volume38en_US
dc.identifier.wosWOS:000537042400001en_US
dc.identifier.wosqualityQ4en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherTaylor & Francis Ltden_US
dc.relation.ispartofBiocatalysis and Biotransformationen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectMagnetic nanoparticlesen_US
dc.subjectsilica coatingen_US
dc.subjectL-asparaginaseen_US
dc.subjectenzyme immobilizationen_US
dc.subjectenhanced stabilityen_US
dc.titlePreparation and characterization of amino and carboxyl functionalized core-shell Fe3O4/SiO2 for L-asparaginase immobilization: A comparison studyen_US
dc.typeArticleen_US

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