Magnetic-propelled Fe3O4-chitosan carriers enhance l-asparaginase catalytic activity: a promising strategy for enzyme immobilization

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dc.authoridKolat, Veli Serkan/0000-0002-8864-5051
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.authorwosidKolat, Veli Serkan/ABI-5280-2020
dc.authorwosidIzgi, tekin/ABH-5655-2020
dc.authorwosidKöytepe, Süleyman/AAA-4168-2021
dc.authorwosidAteş, Burhan/AAA-3730-2021
dc.authorwosidUlu, Ahmet/L-5180-2016
dc.contributor.authorAtes, Burhan
dc.contributor.authorUlu, Ahmet
dc.contributor.authorKoytepe, Suleyman
dc.contributor.authorAli Noma, Samir Abbas
dc.contributor.authorKolat, Veli Serkan
dc.contributor.authorIzgi, Tekin
dc.date.accessioned2024-08-04T20:45:31Z
dc.date.available2024-08-04T20:45:31Z
dc.date.issued2018
dc.departmentİnönü Üniversitesien_US
dc.description.abstractMagnetic-propelled carriers comprising magnetic Fe3O4-chitosan nanoparticles were immobilized with l-asparaginase (l-ASNase). The enzyme displayed enhanced catalytic activity in a weak magnetic field, and thermal and pH stabilities. The conjugated l-ASNase presented higher thermostability and wider range of pH stability in comparison with those of free l-ASNase. Moreover, the reusability of conjugated l-ASNase significantly improved after immobilization and it retained 60.5% of its initial activity after undergoing 16 cycles. The conjugated l-ASNase maintained more than 50% and 48% initial activity after 4 weeks of storage at 4 degrees C and room temperature, respectively. Furthermore, we reveal that the activity of conjugated l-ASNase onto magnetic Fe3O4-chitosan particles increased by about 3-fold in the weak magnetic field at certain frequencies and flux density compared with that of free l-ASNase. Considering these excellent attributes, the magnetic-propelled mechanism in the transporting and activation of l-ASNase can be used by enhancing the catalytic activity, stability, and efficiency in vital implications for medicinal biotechnology.en_US
dc.description.sponsorshipInonu University [FDK-2017-751]en_US
dc.description.sponsorshipAuthors are grateful to the Inonu University (FDK-2017-751).en_US
dc.identifier.doi10.1039/c8ra06346j
dc.identifier.endpage36075en_US
dc.identifier.issn2046-2069
dc.identifier.issue63en_US
dc.identifier.pmid35558460en_US
dc.identifier.scopus2-s2.0-85056115290en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage36063en_US
dc.identifier.urihttps://doi.org/10.1039/c8ra06346j
dc.identifier.urihttps://hdl.handle.net/11616/98526
dc.identifier.volume8en_US
dc.identifier.wosWOS:000448663500024en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherRoyal Soc Chemistryen_US
dc.relation.ispartofRsc Advancesen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCore-Shell Nanoparticlesen_US
dc.subjectIron-Oxide Nanoparticlesen_US
dc.subjectCovalent Immobilizationen_US
dc.subjectChitosan Nanoparticlesen_US
dc.subjectPerformanceen_US
dc.subjectStabilityen_US
dc.subjectLipaseen_US
dc.subjectNanospheresen_US
dc.subjectAdsorptionen_US
dc.subjectSeparationen_US
dc.titleMagnetic-propelled Fe3O4-chitosan carriers enhance l-asparaginase catalytic activity: a promising strategy for enzyme immobilizationen_US
dc.typeArticleen_US

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