Selection of DNA aptamers for the aptamer-assisted magnetic capture of the purified xylanase from Aspergillus niger

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dc.authorscopusid57253263100
dc.authorscopusid57225101720
dc.authorscopusid57215573106
dc.authorscopusid8558322700
dc.contributor.authorDüzel, A.
dc.contributor.authorBora, B.
dc.contributor.authorÖzgen, G.Ö.
dc.contributor.authorEvran, S.
dc.date.accessioned2024-08-25T18:32:24Z
dc.date.available2024-08-25T18:32:24Z
dc.date.issued2024
dc.departmentEge Üniversitesien_US
dc.description.abstractXylanases are a group of enzymes that catalyze the hydrolysis of xylan. Xylanases have wide industrial applications, and they can produced by various organisms. In this study, we aimed to develop aptamers for the capture of xylanase produced by a wild-type Aspergillus niger strain. Xylanase was produced by Aspergillus niger in a 5-liter stirred-tank bioreactor and then purified by column chromatography. Magnetic bead-based SELEX (Systematic Evolution of Ligands by Exponential Enrichment) was performed to select DNA aptamers specific to the purified xylanase. After nine rounds of selection, next-generation sequencing (NGS) analysis was performed. Four aptamers, namely AXYL-1, AXYL-2, AXYL-3, and AXYL-4, were identified for further characterization. The binding properties of the selected aptamers were characterized by fluorescence quenching (FQ) analysis and an enzyme-linked aptamer assay (ELAA). The Kd values were found to be in the low ?M range. Then, each aptamer was immobilized on streptavidin-coated magnetic particles, and the recovery ratio of xylanase was determined. Although AXYL-1 wasn't effective, AXYL-2, AXYL-3, and AXYL-4 were proven to capture the xylanase. The maximum recovery rate of xylanase was found to be approximately 54 %. © 2023 Elsevier B.V.en_US
dc.description.sponsorship115O052; Ege Üniversitesi: FGA-2020-21318en_US
dc.identifier.doi10.1016/j.ijbiomac.2023.128540
dc.identifier.issn0141-8130
dc.identifier.scopus2-s2.0-85178997625en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2023.128540
dc.identifier.urihttps://hdl.handle.net/11454/100219
dc.identifier.volume257en_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherElsevier B.V.en_US
dc.relation.ispartofInternational Journal of Biological Macromoleculesen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.snmz20240825_Gen_US
dc.subjectAptameren_US
dc.subjectProtein purificationen_US
dc.subjectXylanaseen_US
dc.subjectAspergillusen_US
dc.subjectBinding energyen_US
dc.subjectColumn chromatographyen_US
dc.subjectFluorescence quenchingen_US
dc.subjectPurificationen_US
dc.subjectAptamersen_US
dc.subjectAspergillus nigeren_US
dc.subjectCatalyseen_US
dc.subjectDna aptameren_US
dc.subjectMagnetic beadsen_US
dc.subjectMagnetic captureen_US
dc.subjectProtein purificationen_US
dc.subjectStirred tank bioreactorsen_US
dc.subjectWild typesen_US
dc.subjectXylanasesen_US
dc.subjectEnzymesen_US
dc.subjectaptameren_US
dc.subjectmagnetic nanoparticleen_US
dc.subjectstreptavidinen_US
dc.subjectxylan endo 1,3 beta xylosidaseen_US
dc.subjectArticleen_US
dc.subjectAspergillus nigeren_US
dc.subjectAXYL 1 geneen_US
dc.subjectAXYL 2 geneen_US
dc.subjectAXYL 3 geneen_US
dc.subjectAXYL 4 geneen_US
dc.subjectcolumn chromatographyen_US
dc.subjectDNA determinationen_US
dc.subjectenzyme assayen_US
dc.subjectenzyme linked aptamer assayen_US
dc.subjectfluorescence analysisen_US
dc.subjectgeneen_US
dc.subjecthigh throughput sequencingen_US
dc.subjectnonhumanen_US
dc.subjectprotein analysisen_US
dc.subjectprotein purificationen_US
dc.subjectsystematic evolution of ligands by exponential enrichment aptamer techniqueen_US
dc.titleSelection of DNA aptamers for the aptamer-assisted magnetic capture of the purified xylanase from Aspergillus nigeren_US
dc.typeArticleen_US

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