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Tailoring of Recombinant Fdh: Effect of Histidine Tag Location on Solubility and Catalytic Properties of Chaetomium Thermophilum Formate Dehydrogenase (Ctfdh)

dc.authorid Alpdagtas, Saadet/0000-0002-8322-2658
dc.authorid Cakar, Mehmet Mervan/0000-0001-6972-5841
dc.authorscopusid 57208581332
dc.authorscopusid 56403428200
dc.authorscopusid 57201393763
dc.authorscopusid 23471733900
dc.authorwosid Alpdağtaş, Saadet/Aaa-3008-2021
dc.authorwosid Binay, Baris/Abb-7968-2021
dc.contributor.author Esen, Hacer
dc.contributor.author Alpdagtas, Saadet
dc.contributor.author Cakar, Mehmet Mervan
dc.contributor.author Binay, Baris
dc.date.accessioned 2025-05-10T17:34:14Z
dc.date.available 2025-05-10T17:34:14Z
dc.date.issued 2019
dc.department T.C. Van Yüzüncü Yıl Üniversitesi en_US
dc.department-temp [Esen, Hacer] Gebze Tech Univ, Dept Chem Engn, Kocaeli, Turkey; [Alpdagtas, Saadet] Van Yuzuncu Yil Univ, Fac Sci, Dept Biol, Van, Tusba, Turkey; [Cakar, Mehmet Mervan] Gebze Tech Univ, Dept Mol Biol & Genet, Kocaeli, Turkey; [Binay, Baris] Gebze Tech Univ, Dept Bioengn, Istanbul Caddesi PK 141, TR-41400 Kocaeli, Turkey en_US
dc.description Alpdagtas, Saadet/0000-0002-8322-2658; Cakar, Mehmet Mervan/0000-0001-6972-5841 en_US
dc.description.abstract Several protein expression systems can be used to get enzymes in required quantities and study their functions. Incorporating a polyhistidine tag is a beneficial way of getting various enzymes such as FDHs for industrial applications. The NAD(+) dependent formate dehydrogenase from Chaetomium thermophilum (CtFDH) can be utilized for interconversion of formate to carbon dioxide coupled with the conversion of NAD(+) to NADH. In this study, N-terminal His tagged CtFDH (N-CtFDH) and C-terminal His tagged CtFDH (C-CtFDH) was constructed to learn the effect of His tag location on the activity and kinetic parameters of the enzyme. The solubility of proteins was not affected by tag position, however, an interference on the N-terminal region caused a deterioration in specific activity and the kinetic ability of enzyme. The obtained results indicated that the C-terminus of the enzyme is an appropriate region for tag engineering. The C-CtFDH has an approximately three-fold larger specific activity and two-fold higher catalytic efficiency than N-CtFDH. The results suggest that insertion of a His-tag at the N-terminal or C-terminal end of CtFDH has different effects on the protein and the N-terminal fragment of the protein is crucial for the function of CtFDH. en_US
dc.description.woscitationindex Science Citation Index Expanded - Conference Proceedings Citation Index - Science
dc.identifier.doi 10.1080/10826068.2019.1599394
dc.identifier.endpage 534 en_US
dc.identifier.issn 1082-6068
dc.identifier.issn 1532-2297
dc.identifier.issue 5 en_US
dc.identifier.pmid 31030612
dc.identifier.scopus 2-s2.0-85065215493
dc.identifier.scopusquality Q3
dc.identifier.startpage 529 en_US
dc.identifier.uri https://doi.org/10.1080/10826068.2019.1599394
dc.identifier.uri https://hdl.handle.net/20.500.14720/13723
dc.identifier.volume 49 en_US
dc.identifier.wos WOS:000475681400015
dc.identifier.wosquality Q3
dc.language.iso en en_US
dc.publisher Taylor & Francis inc en_US
dc.relation.ispartof 1st International Eurasia Biochemical Approaches and Technologies Meeting (EBAT) -- OCT 26-30, 2018 -- Antalya, TURKEY en_US
dc.relation.publicationcategory Konferans Öğesi - Uluslararası - Kurum Öğretim Elemanı en_US
dc.rights info:eu-repo/semantics/closedAccess en_US
dc.subject Catalytic Property en_US
dc.subject Chaetomium Thermophilum en_US
dc.subject Formate Dehydrogenase en_US
dc.subject His Tag Position en_US
dc.subject N- Or C-Terminal en_US
dc.subject Solubility en_US
dc.title Tailoring of Recombinant Fdh: Effect of Histidine Tag Location on Solubility and Catalytic Properties of Chaetomium Thermophilum Formate Dehydrogenase (Ctfdh) en_US
dc.type Conference Object en_US

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