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

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dc.authoridbora, burhan/0000-0002-9982-2922
dc.authoridDUZEL, Ahmet/0000-0003-4106-4548
dc.contributor.authorDuzel, Ahmet
dc.contributor.authorBora, Burhan
dc.contributor.authorOzgen, Gaye Ongen
dc.contributor.authorEvran, Serap
dc.date.accessioned2025-03-23T19:41:28Z
dc.date.available2025-03-23T19:41:28Z
dc.date.issued2024
dc.departmentSinop Üniversitesi
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 mu 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 %.
dc.description.sponsorshipEge University Scientific Research Projects Coordination Unit [FGA-2020-21318]; Turkish Scientific and Technological Research Institution through TUEBITAK 1003 project [115O052]
dc.description.sponsorshipThis work supported by Ege University Scientific Research Projects Coordination Unit (Project No: FGA-2020-21318) and partially supported by the Turkish Scientific and Technological Research Institution through TUEBITAK 1003 project (Project No: 115O052). We also thank to TUEBITAK-MAM (Turkish Scientific and Technological Research Institution-Marmara Research Center) for supplying Aspergillus niger strain in this work.
dc.identifier.doi10.1016/j.ijbiomac.2023.128540
dc.identifier.issn0141-8130
dc.identifier.issn1879-0003
dc.identifier.pmid38061523
dc.identifier.scopus2-s2.0-85178997625
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2023.128540
dc.identifier.urihttps://hdl.handle.net/11486/6592
dc.identifier.volume257
dc.identifier.wosWOS:001134312000001
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_20250323
dc.subjectXylanase
dc.subjectAptamer
dc.subjectProtein purification
dc.titleSelection of DNA aptamers for the aptamer-assisted magnetic capture of the purified xylanase from Aspergillus niger
dc.typeArticle

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