Newly Synthesized Multifunctional Biopolymer Coated Magnetic Core/Shell Fe3O4@Au Nanoparticles for Evaluation of L-asparaginase Immobilization

dc.authoridUlu, Ahmet/0000-0002-4447-6233
dc.authoridTarhan, Tuba/0000-0003-2656-4464
dc.authoridAtes, Burhan/0000-0001-6080-229X
dc.authoridDik, Gamze/0000-0003-4798-8127
dc.authorwosidUlu, Ahmet/L-5180-2016
dc.contributor.authorTarhan, Tuba
dc.contributor.authorDik, Gamze
dc.contributor.authorUlu, Ahmet
dc.contributor.authorTural, Bilsen
dc.contributor.authorTural, Servet
dc.contributor.authorAtes, Burhan
dc.date.accessioned2024-08-04T20:53:08Z
dc.date.available2024-08-04T20:53:08Z
dc.date.issued2023
dc.departmentİnönü Üniversitesien_US
dc.description.abstractThe immobilization strategy can promote greater enzyme utilization in applications by improving the overall stability and reusability of the enzyme. In this work, the L-asparaginase (L-ASNase) obtained from Escherichia coli was chosen as a model enzyme and immobilized onto the Fe3O4@Au-carboxymethyl chitosan (CMC) magnetic nanoparticles (MNPs) through adsorption. TEM, SEM, FT-IR, XRD, EDS, and TGA analyses were performed to examine the structure with and without L-ASNase. The yield of immobilized L-ASNase on Fe3O4@Au-CMC was found to be 68%. The biochemical properties such as optimum pH, optimum temperature, reusability, and thermal stability of the Fe3O4@Au-CMC/L-ASNase were comprehensively investigated. For instance, Fe3O4@Au-CMC/L-ASNase reached maximum activity at pH 7.0 and the optimum temperature was found to be 50 degrees C. The noticeably lower Ea value of the Fe3O4@Au-CMC/L-ASNase revealed the enhanced catalytic activity of this enzyme after immobilization. The Km and Vmax values were 3.27 +/- 0.48 mM, and 51.54 +/- 0.51 mu mol min(-1) for Fe3O4@Au-CMC/L-ASNase, respectively, which means good substrate affinity. The Fe3O4@Au-CMC/L-ASNase retained 65% of its initial activity even after 90 min at 60 degrees C. Moreover, it maintained more than 75% of its original activity after 10 cycles, indicating its excellent reusability. The results obtained suggested that this investigation highlights the use of MNPs as a support for the development of more economical and sustainable immobilized enzyme systems.en_US
dc.description.sponsorshipScientific Research Projects Unit of Inonu University [FBG-2021-2731]en_US
dc.description.sponsorshipThe work team would like to thank the partial financial provided by the Scientific Research Projects Unit of Inonu University (Project number: FBG-2021-2731).en_US
dc.identifier.doi10.1007/s11244-022-01742-y
dc.identifier.endpage591en_US
dc.identifier.issn1022-5528
dc.identifier.issn1572-9028
dc.identifier.issue9-12en_US
dc.identifier.scopus2-s2.0-85141947662en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage577en_US
dc.identifier.urihttps://doi.org/10.1007/s11244-022-01742-y
dc.identifier.urihttps://hdl.handle.net/11616/100994
dc.identifier.volume66en_US
dc.identifier.wosWOS:000885717300001en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringer/Plenum Publishersen_US
dc.relation.ispartofTopics in Catalysisen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectFe3O4@Auen_US
dc.subjectCarboxymethyl chitosanen_US
dc.subjectEnzyme carrieren_US
dc.subjectL-asparaginase immobilizationen_US
dc.subjectEnhanced stabilityen_US
dc.titleNewly Synthesized Multifunctional Biopolymer Coated Magnetic Core/Shell Fe3O4@Au Nanoparticles for Evaluation of L-asparaginase Immobilizationen_US
dc.typeArticleen_US

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