Design of near-infrared light induced functionalized upconverting nanoparticles as support in enzyme immobilization: Enhanced biocatalyst activity and stability

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dc.contributor.authorUlu, Ahmet
dc.contributor.authorNoma, Samir Abbas Ali
dc.contributor.authorKurucay, Ali
dc.contributor.authorTopel, Seda Demirel
dc.contributor.authorAsilturk, Meltem
dc.contributor.authorAtes, Burhan
dc.date.accessioned2026-04-04T13:35:03Z
dc.date.available2026-04-04T13:35:03Z
dc.date.issued2025
dc.departmentİnönü Üniversitesi
dc.description.abstractIn this study, we hypothesized that the emission of upconverted nanoparticles (UCNP) can trigger PEG-L-ASNase (P-Lase) activity through Forster Resonance Energy Transfer under near-infrared (NIR) irradiation. To enhance stability and activity of P-Lase, it was immobilized on functionalized NaYF4:Yb3+, Er3+, Nd3+. Upon immobilization, the obtained NaYF4:Yb3+, Er3+, Nd3+/GPTMS-P-Lase exhibited excellent pH stability, thermal stability, metal ions or organic solvent tolerance, and storage stability. The relative activity of NaYF4:Yb3+, Er3+, Nd3+/ GPTMS-P-Lase had about 65 % after 20 cycles and maintained 68 % and 59 % at +4 and 25 degrees C, respectively, after 4 weeks. Furthermore, in vitro cytotoxicity and hemolysis tests confirmed that the synthesized UCNPs were biocompatible. Most importantly, the activity of P-Lase was enhanced >= 4-fold under suitable NIR irradiation. It is reasonable to believe that this investigation may supply a novel technique to trigger the catalytic efficiency of P-Lase and may have promising application in leukemia treatment.
dc.description.sponsorshipThe 2515-COST (European Cooperation in Science and Technology (TUMIEE-COST Action CA17126) ) of the Scientific and Technological Research Council of Turkiye [119Z962]
dc.description.sponsorshipThis study was funded by grant from 2515-COST (European Cooperation in Science and Technology (TUMIEE-COST Action CA17126) ) of the Scientific and Technological Research Council of Turkiye (119Z962) .
dc.identifier.doi10.1016/j.ijbiomac.2025.140581
dc.identifier.issn0141-8130
dc.identifier.issn1879-0003
dc.identifier.pmid39900163
dc.identifier.scopus2-s2.0-85216788474
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2025.140581
dc.identifier.urihttps://hdl.handle.net/11616/109586
dc.identifier.volume302
dc.identifier.wosWOS:001422600900001
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherElsevier
dc.relation.ispartofInternational Journal of Biological Macromolecules
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WOS_20250329
dc.subjectUpconverting nanoparticles
dc.subjectSurface modification
dc.subjectL-Asparaginase immobilization
dc.subjectNear-infrared
dc.subjectTriggered activity
dc.titleDesign of near-infrared light induced functionalized upconverting nanoparticles as support in enzyme immobilization: Enhanced biocatalyst activity and stability
dc.typeArticle

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