Magnetic Fe3O4@MCM-41 core-shell nanoparticles functionalized with thiol silane for efficient l-asparaginase 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.authorwosidNOMA, SAMIR/ABH-1773-2021
dc.authorwosidKöytepe, Süleyman/AAA-4168-2021
dc.authorwosidAteş, Burhan/AAA-3730-2021
dc.authorwosidUlu, Ahmet/L-5180-2016
dc.contributor.authorUlu, Ahmet
dc.contributor.authorNoma, Samir Abbas Ali
dc.contributor.authorKoytepe, Suleyman
dc.contributor.authorAtes, Burhan
dc.date.accessioned2024-08-04T20:44:34Z
dc.date.available2024-08-04T20:44:34Z
dc.date.issued2018
dc.departmentİnönü Üniversitesien_US
dc.description.abstractL-Asparaginase (L-ASNase) is a vital enzyme for medical treatment and food industry. Here, we assessed the use of Fe3O4@Mobil Composition of Matter No. 41 (MCM-41) magnetic nanoparticles as carrier matrix for L-ASNase immobilization. In addition, surface of Fe3O4@MCM-41 magnetic nanoparticles was functionalized with 3-mercaptopropyltrimethoxysilane (MPTMS) to enhance stability of L-ASNase. The chemical structure, thermal properties, magnetic profile and morphology of the thiol-functionalized Fe3O4@MCM-41 magnetic nanoparticles were characterized with Fourier transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA), differential thermal analysis (DTA), differential scanning calorimetry (DSC), vibrating sample magnetometer (VSM), scanning electron microscope (SEM), energy dispersive X-ray (EDX) spectroscopy and zeta-potential measurement. L-ASNase was covalently immobilized onto the thiol-functionalized Fe3O4@MCM-41 magnetic nanoparticles. The properties of the immobilized enzyme, including optimum pH, temperature, kinetic parameters, thermal stability, reusability and storage stability were investigated and compared to free one. Immobilized enzyme was found to be stable over a wide range of pH and temperature range than free enzyme. The immobilized L-ASNase also showed higher thermal stability after 180 min incubation at 50 degrees C. The immobilized enzyme still retained 63% of its original activity after 16 times of reuse. The Km value for the immobilized enzyme was 1.15-fold lower than the free enzyme, which indicates increased affinity for the substrate. Additionally, the immobilized enzyme was active over 65% and 53% after 30 days of storage at 4 degrees C and room temperature (similar to 25 degrees C), respectively. Thereby, the results confirmed that thiol-functionalized Fe3O4@MCM-41 magnetic nanoparticles had high efficiency for L-ASNase immobilization and improved stability of L-ASNase.en_US
dc.description.sponsorshipInonu University [FDK-751]en_US
dc.description.sponsorshipThe work was partially supported by Inonu University [Grant number: FDK-751].en_US
dc.identifier.doi10.1080/21691401.2018.1478422
dc.identifier.endpage1045en_US
dc.identifier.issn2169-1401
dc.identifier.issn2169-141X
dc.identifier.pmid29873527en_US
dc.identifier.scopus2-s2.0-85048094503en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage1035en_US
dc.identifier.urihttps://doi.org/10.1080/21691401.2018.1478422
dc.identifier.urihttps://hdl.handle.net/11616/98321
dc.identifier.volume46en_US
dc.identifier.wosWOS:000459181400099en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherTaylor & Francis Ltden_US
dc.relation.ispartofArtificial Cells Nanomedicine and Biotechnologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectFe3O4@MCM-41en_US
dc.subjectmagnetic nanoparticlesen_US
dc.subjectthiol-functionalizeden_US
dc.subjectL-asparaginaseen_US
dc.subjectimmobilizationen_US
dc.titleMagnetic Fe3O4@MCM-41 core-shell nanoparticles functionalized with thiol silane for efficient l-asparaginase immobilizationen_US
dc.typeArticleen_US

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