Near-infrared inducible supports in bio-catalysts design: A useful and versatile tool in enhancement of enzyme activity

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dc.authoridGürses, Canbolat/0000-0002-4085-0224
dc.authorwosidGürses, Canbolat/AAA-6825-2019
dc.contributor.authorNoma, Samir Abbas Ali
dc.contributor.authorDik, Gamze
dc.contributor.authorGurses, Canbolat
dc.contributor.authorKurucay, Ali
dc.contributor.authorTopel, Seda Demirel
dc.contributor.authorUlu, Ahmet
dc.contributor.authorAsiltuerk, Meltem
dc.date.accessioned2024-08-04T20:55:55Z
dc.date.available2024-08-04T20:55:55Z
dc.date.issued2024
dc.departmentİnönü Üniversitesien_US
dc.description.abstractImmobilized enzymes have encountered two main challenges: Reduced enzyme activity compared to free enzymes and exhausted immobilized enzymes due to reusability. Herein, we suggested a promising activity enhancement strategy to overcome these challenges. The emission from upconversion nanoparticles (UCNPs) under near-infrared (NIR) excitation can increase the activity of PEG-L-ASNase due to Forster Resonance Energy Transfer. For this purpose, UCNPs were initially synthesized using the hydrothermal method. Subsequently, these UCNPs were functionalized with a polycationic polymer, branched polyethyleneimine (PEI), and the immobilization of PEG-L-ASNase was achieved through adsorption. We preliminarily explored the parameters such as enzyme concentration, incubation time, pH, temperature, reusability, storage stability, and kinetic study, etc. Further, the in vitro biocompatibility, hemolytic behavior, and anticancer activity of the produced UCNPs were also analyzed as crucial parameters. The results showed the pH durance, thermal and storage stability of the immobilized PEG-L-ASNases were enhanced. The immobilized PEG-L-ASNases maintained their activity to >= 55 % after 20 cycles. Enzyme immobilization led to a decrease in Km and Vmax compared to PEG-L-ASNase. In vitro assays revealed that immobilized enzyme further reduced the proliferation of human leukemia cell line (HL-60) upon NIR irradiation exposure but did not cause toxicity. This research may provide a new strategy to promote the catalytic activity of L-ASNase and demonstrates its potential application on human leukemia cells. Finally, these outcomes are valuable for the use of NIR induction in enzymatic reactions.en_US
dc.description.sponsorship2515 -COST (European Cooperation in Science and Technology (TUMIEE-COST Action of the Scientific and Technological Research Council of Turkiye [119Z962]en_US
dc.description.sponsorshipThis research work was supported 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) .en_US
dc.identifier.doi10.1016/j.mcat.2024.114130
dc.identifier.issn2468-8231
dc.identifier.scopus2-s2.0-85190066598en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.urihttps://doi.org/10.1016/j.mcat.2024.114130
dc.identifier.urihttps://hdl.handle.net/11616/101928
dc.identifier.volume560en_US
dc.identifier.wosWOS:001234814500001en_US
dc.identifier.wosqualityN/Aen_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relation.ispartofMolecular Catalysisen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectLanthanide -doped nanoparticlesen_US
dc.subjectLight -induced supportsen_US
dc.subjectNearen_US
dc.subjectinfrared irradiationen_US
dc.subjectForster resonance energy transferen_US
dc.subjectTriggered activityen_US
dc.subjectThermostabilityen_US
dc.subjectReusabilityen_US
dc.titleNear-infrared inducible supports in bio-catalysts design: A useful and versatile tool in enhancement of enzyme activityen_US
dc.typeArticleen_US

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