The Carboxylated Multi-walled Carbon Nanotubes/l-Asparaginase Doped Calcium-Alginate Beads: Structural and Biocatalytic Characterization

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dc.authoridAteş, Burhan/0000-0001-6080-229X
dc.authoridUlu, Ahmet/0000-0002-4447-6233
dc.authoridsaygili, eyup ilker/0000-0002-0102-4237
dc.authoridKaraman, Muhammet/0000-0002-0155-3390
dc.authorwosidAteş, Burhan/AAA-3730-2021
dc.authorwosidUlu, Ahmet/L-5180-2016
dc.authorwosidsaygili, eyup ilker/X-1954-2019
dc.authorwosidKaraman, Muhammet/AAG-4541-2019
dc.contributor.authorUlu, Ahmet
dc.contributor.authorKaraman, Muhammet
dc.contributor.authorYapici, Fatma
dc.contributor.authorNaz, Mehmet
dc.contributor.authorSayin, Selin
dc.contributor.authorSaygili, Eyup Ilker
dc.contributor.authorAtes, Burhan
dc.date.accessioned2024-08-04T20:47:02Z
dc.date.available2024-08-04T20:47:02Z
dc.date.issued2020
dc.departmentİnönü Üniversitesien_US
dc.description.abstractThe calcium-alginate/multi-walled carbon nanotube hybrid beads (Ca-ALG/MWCNT-COOH) as a novel kind of matrix were fabricated and characterized in detailed. l-Asparaginase (l-ASNase), which is important chemotherapeutic enzyme-drug in leukemia, was immobilized on the Ca-ALG/MWCNT-COOH hybrid beads. To the best of our knowledge, this is the first study using Ca-ALG/MWCNT-COOH hybrid beads for l-ASNase immobilization. Our characterization investigations displayed that the hybridization between ALG and MWCNT-COOH caused significant changes on the surface morphology and structure. ALG of 0.5% (w/v), CaCl2 of 0.2 M concentration, enzyme of 187.5 U and bead size of 2 mm was found to be best with respect to enzyme loading efficiency. The enzyme was loaded a high yield (97.0%) on these hybrid beads. Remarkably, the tolerance of immobilized enzyme developed towards temperature and pH changes. The maximum activity for the free enzyme was observed at 35 degrees C, pH 7.5, whereas the immobilized enzyme showed maximum activity at 45 degrees C pH 8.5. After immobilization, storage stability of enzyme improved and retained more than 70% of its initial activity after 4 weeks at ~ 30 degrees C as compared with free enzyme which showed only 20% of residual activity. After immobilization, Km value decreased 1.27-fold compared to free counterpart, indicating increased the affinity between the substrate and enzyme. Moreover, immobilized enzyme maintained more than 36% of its original activity even after consecutive 14 reuse. As result, it is worthy of noting that this kind of hybrid materials may become a promising support material for the immobilization of commercial enzymes in areas such as industrial and medical. Graphicen_US
dc.identifier.doi10.1007/s10562-019-03069-y
dc.identifier.endpage1691en_US
dc.identifier.issn1011-372X
dc.identifier.issn1572-879X
dc.identifier.issue6en_US
dc.identifier.scopus2-s2.0-85076897310en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage1679en_US
dc.identifier.urihttps://doi.org/10.1007/s10562-019-03069-y
dc.identifier.urihttps://hdl.handle.net/11616/99112
dc.identifier.volume150en_US
dc.identifier.wosWOS:000528850500014en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofCatalysis Lettersen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCa-alginateen_US
dc.subjectMulti-walled carbon nanotubesen_US
dc.subjectHybrid beadsen_US
dc.subjectl-Asparaginaseen_US
dc.subjectImmobilizationen_US
dc.subjectEncapsulationen_US
dc.titleThe Carboxylated Multi-walled Carbon Nanotubes/l-Asparaginase Doped Calcium-Alginate Beads: Structural and Biocatalytic Characterizationen_US
dc.typeArticleen_US

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