A New Design to Enhance the Enzyme Activities: Investigation of L-Asparaginase Catalytic Performance by IMAC Effect on g-C3N4 Nanolayers

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dc.authoridhttps://orcid.org/0000-0003-2807-0425
dc.authorscopusid36088420200
dc.authorwosidAAM-8078-2020
dc.authorwosidDRG-0686-2022
dc.authorwosid57202381427
dc.authorwosidABF-4791-2020
dc.authorwosidDIR-4597-2022
dc.contributor.authorSert, Buse
dc.contributor.authorAcet, Ömür
dc.contributor.authorNoma, Samir Abbas Ali
dc.contributor.authorOsman, Bilgen
dc.contributor.authorOdabaşı, Mehmet
dc.contributor.authorOcakoğlu, Kasım
dc.date.accessioned2024-08-06T11:35:24Z
dc.date.available2024-08-06T11:35:24Z
dc.date.issued2024
dc.departmentFakülteler, Mühendislik Fakültesi, Mühendislik Temel Bilimleri Bölümü
dc.description.abstractRecently, graphite carbon nitride (g-C3N4) has come to the fore as a new material with its carbon-based two-dimensional structure, simple preparation procedure, and excellent physicochemical stability properties. This study aims to investigate the activity and kinetic studies of the L-asparaginase enzyme via immobilized metal ion affinity chromatography (IMAC) process of g-C3N4 nanolayers. Firstly, g-C3N4 nanolayers were synthetized and Ni2+ ions were binded their surfaces. The synthesized samples were investigated by SEM, ICP-MS, XRD, and FTIR. The highest L-ASNase adsorption on Ni2+-g-C3N4 nanostructures was 444.1 mg/g, at 3 mg/mL L-ASNase concentration. Optimal medium conditions for L-ASNase adsorption occurred at pH 8.0 and 25 °C. The immobilized enzyme showed improved stability relating to the soluble enzyme in extreme situations. On the other hand, the storage stability and reusability of the immobilized enzyme were found to be approximately 64 and 53% of the original activity after 29 days at room temperature and 10 cycles, respectively. From the Michaelis–Menten constants Km and Vmax, both of them decreased after immobilization compare to the free one. The obtained outcomes showed that the g-C3N4 is a suitable matrix for L-asparaginase immobilization with ideal catalytic efficiency and improved stability.
dc.identifier.citationSert, B., Acet, Ö., Noma, S.A.A., Osman, B., Odabaşı, M. ve Ocakoğlu, K. (2024). A New Design to Enhance the Enzyme Activities: Investigation of L-Asparaginase Catalytic Performance by IMAC Effect on g-C3N4 Nanolayers. Catal Lett 154 (4), 1547–1557. https://doi.org/10.1007/s10562-023-04405-z
dc.identifier.doi10.1007/s10562-023-04405-z
dc.identifier.endpage1557en_US
dc.identifier.issn1011-372X
dc.identifier.issn1572-879X
dc.identifier.issue4en_US
dc.identifier.scopus2-s2.0-85164194690
dc.identifier.scopusqualityQ2
dc.identifier.startpage1547en_US
dc.identifier.urihttps://link.springer.com/article/10.1007/s10562-023-04405-z
dc.identifier.urihttps://hdl.handle.net/20.500.13099/328
dc.identifier.volume154en_US
dc.identifier.wosWOS:001025705800001
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherSpringer Link
dc.relation.ispartofCatalysis Letters
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectGraphite carbon nitride
dc.subjectNanolayers
dc.subjectL-ASNase
dc.subjectEnzyme activity
dc.subjectImmobilization
dc.titleA New Design to Enhance the Enzyme Activities: Investigation of L-Asparaginase Catalytic Performance by IMAC Effect on g-C3N4 Nanolayers
dc.typeArticle

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