Newly Synthesized Multifunctional Biopolymer Coated Magnetic Core/Shell Fe3O4@Au Nanoparticles for Evaluation of L-asparaginase Immobilization
dc.authorid | Ulu, Ahmet/0000-0002-4447-6233 | |
dc.authorid | Tarhan, Tuba/0000-0003-2656-4464 | |
dc.authorid | Ates, Burhan/0000-0001-6080-229X | |
dc.authorid | Dik, Gamze/0000-0003-4798-8127 | |
dc.authorwosid | Ulu, Ahmet/L-5180-2016 | |
dc.contributor.author | Tarhan, Tuba | |
dc.contributor.author | Dik, Gamze | |
dc.contributor.author | Ulu, Ahmet | |
dc.contributor.author | Tural, Bilsen | |
dc.contributor.author | Tural, Servet | |
dc.contributor.author | Ates, Burhan | |
dc.date.accessioned | 2024-08-04T20:53:08Z | |
dc.date.available | 2024-08-04T20:53:08Z | |
dc.date.issued | 2023 | |
dc.department | İnönü Üniversitesi | en_US |
dc.description.abstract | The 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.sponsorship | Scientific Research Projects Unit of Inonu University [FBG-2021-2731] | en_US |
dc.description.sponsorship | The 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.doi | 10.1007/s11244-022-01742-y | |
dc.identifier.endpage | 591 | en_US |
dc.identifier.issn | 1022-5528 | |
dc.identifier.issn | 1572-9028 | |
dc.identifier.issue | 9-12 | en_US |
dc.identifier.scopus | 2-s2.0-85141947662 | en_US |
dc.identifier.scopusquality | Q2 | en_US |
dc.identifier.startpage | 577 | en_US |
dc.identifier.uri | https://doi.org/10.1007/s11244-022-01742-y | |
dc.identifier.uri | https://hdl.handle.net/11616/100994 | |
dc.identifier.volume | 66 | en_US |
dc.identifier.wos | WOS:000885717300001 | en_US |
dc.identifier.wosquality | Q2 | en_US |
dc.indekslendigikaynak | Web of Science | en_US |
dc.indekslendigikaynak | Scopus | en_US |
dc.language.iso | en | en_US |
dc.publisher | Springer/Plenum Publishers | en_US |
dc.relation.ispartof | Topics in Catalysis | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Fe3O4@Au | en_US |
dc.subject | Carboxymethyl chitosan | en_US |
dc.subject | Enzyme carrier | en_US |
dc.subject | L-asparaginase immobilization | en_US |
dc.subject | Enhanced stability | en_US |
dc.title | Newly Synthesized Multifunctional Biopolymer Coated Magnetic Core/Shell Fe3O4@Au Nanoparticles for Evaluation of L-asparaginase Immobilization | en_US |
dc.type | Article | en_US |