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The function of the enzyme was confirmed, as aldehyde-oxidation activity with the native redox partner ferredoxin, as well as with artificial redox partners. Optimization of the medium did increase specific activity of the heterologous protein, which is active over a wide temperature and pH range, and is able to oxidize a wide variety of aldehydes to their corresponding acids.</field><field name="allMeta">Diese Studie konzentrierte sich auf die vielseitige AOR von Thermoanaerobacter sp. Stamm X514 (AORX514), die durch Produktion einer His-markierten Version in Thermoanaerobacter kivui biochemisch charakterisiert wurde. Die Funktion des Enzyms wurde bestätigt, da die Aldehyd-Oxidationsaktivität sowohl mit dem nativen Redoxpartner Ferredoxin als auch mit künstlichen Redoxpartnern nachgewiesen wurde. 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W. Adams (Department of Biochemistry and Molecular Biology)</field><field name="allMeta">[{"name":"Basen, Mirko","affil":"Institute of Biological Sciences, Universität Rostock"},{"name":"Adams, Michael W. W.","affil":"Department of Biochemistry and Molecular Biology"}]</field><field name="allMeta">Dissertation, Universität Rostock, 2024</field><field name="allMeta">vorgelegt von Laura Sofie Nissen</field><field name="allMeta">Basen, Mirko</field><field name="allMeta">Institute of Biological Sciences, Universität Rostock</field><field name="allMeta">Adams, Michael W. 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Mathematisch-Naturwissenschaftliche Fakultät</field><field name="allMeta">Mathematisch-Natur-&lt;br /&gt;wissenschaftliche Fakultät</field><field name="allMeta">Uni.Rostock.Fakultaet.MNF</field><field name="allMeta">http://d-nb.info/gnd/2147083-2</field><field name="category">licenseinfo:work</field><field name="category.top">licenseinfo:work</field><field name="allMeta">Werk</field><field name="allMeta">work</field><field name="category">licenseinfo:work.rightsreserved</field><field name="category.top">licenseinfo:work.rightsreserved</field><field name="allMeta">alle Rechte vorbehalten</field><field name="allMeta">all rights reserved</field><field name="allMeta">/creativecommons/r/reserved/0.9/88x31.png</field><field name="allMeta">[DE-28]Urheberrechtsschutz 1.0$gRights Statements$uhttp://rightsstatements.org/vocab/InC/1.0/</field><field name="allMeta">http://rightsstatements.org/vocab/InC/1.0/</field><field name="allMeta">http://rightsstatements.org/vocab/InC/1.0/</field><field name="category">licenseinfo:deposit</field><field name="category.top">licenseinfo:deposit</field><field name="allMeta">Veröffentlichungsgenehmigung</field><field name="allMeta">permission to store</field><field name="category">licenseinfo:deposit.rightsgranted</field><field name="category.top">licenseinfo:deposit.rightsgranted</field><field name="allMeta">Nutzungsrechte erteilt</field><field name="allMeta">rights granted</field><field name="category">licenseinfo:metadata</field><field name="category.top">licenseinfo:metadata</field><field name="allMeta">Lizenzen für Metadaten</field><field name="category">licenseinfo:metadata.cc0</field><field name="category.top">licenseinfo:metadata.cc0</field><field name="allMeta">Lizenz Metadaten: CC0</field><field name="allMeta">license metadata: CC0</field><field name="allMeta">/creativecommons/p/zero/1.0/88x31.png</field><field name="allMeta">https://creativecommons.org/publicdomain/zero/1.0/</field><field name="category">accesscondition:openaccess</field><field name="category.top">accesscondition:openaccess</field><field name="allMeta">frei zugänglich (Open Access)</field><field name="allMeta">open access</field><field name="allMeta">http://purl.org/coar/access_right/c_abf2</field><field name="allMeta">OA</field><field name="allMeta">free</field><field name="allMeta">info:eu-repo/semantics/openAccess</field><field name="allMeta">[DE-28]Open Access$gControlled Vocabulary for Access Rights$uhttp://purl.org/coar/access_right/c_abf2</field><field name="category">rfc5646:en</field><field name="category.top">rfc5646:en</field><field name="allMeta">Englisch</field><field name="allMeta">English</field><field name="allMeta">eng</field><field name="allMeta">eng</field><field name="mods.title">Biochemical characterization of aldehyde:ferredoxin oxidoreductase from the thermophilic bacterium Thermoanaerobacter sp. strain X514</field><field name="mods.title.main">Biochemical characterization of aldehyde:ferredoxin oxidoreductase from the thermophilic bacterium Thermoanaerobacter sp. strain X514</field><field name="mods.title.subtitle"></field><field name="mods.nameIdentifier">gnd:1372417885</field><field name="mods.nameIdentifier">gnd:38329-6</field><field name="mods.nameIdentifier">gnd:2147083-2</field><field name="mods.nameIdentifier.top">gnd:1372417885</field><field name="mods.nameIdentifier.top">gnd:38329-6</field><field name="mods.nameIdentifier.top">gnd:2147083-2</field><doc><field name="id">rosdok_disshab_0000003293-d1118548e54</field><field name="mods.nameIdentifier">gnd:1372417885</field><field name="mods.name">Laura Sofie Nissen</field><field name="mods.name.top">Laura Sofie Nissen</field></doc><doc><field name="id">rosdok_disshab_0000003293-d1118548e68</field><field name="mods.name">Mirko Basen</field><field name="mods.name.top">Mirko Basen</field></doc><doc><field name="id">rosdok_disshab_0000003293-d1118548e79</field><field name="mods.name">Michael W. W. Adams</field><field name="mods.name.top">Michael W. W. Adams</field></doc><doc><field name="id">rosdok_disshab_0000003293-d1118548e91</field><field name="mods.nameIdentifier">gnd:38329-6</field><field name="mods.name">Universität Rostock</field><field name="mods.name.top">Universität Rostock</field></doc><doc><field name="id">rosdok_disshab_0000003293-d1118548e104</field><field name="mods.nameIdentifier">gnd:2147083-2</field><field name="mods.name">Universität Rostock. Mathematisch-Naturwissenschaftliche Fakultät</field><field name="mods.name.top">Universität Rostock. Mathematisch-Naturwissenschaftliche Fakultät</field></doc><field name="mods.name">Laura Sofie Nissen</field><field name="mods.name">Mirko Basen</field><field name="mods.name">Michael W. W. Adams</field><field name="mods.name">Universität Rostock</field><field name="mods.name">Universität Rostock. Mathematisch-Naturwissenschaftliche Fakultät</field><field name="mods.name.top">Laura Sofie Nissen</field><field name="mods.name.top">Mirko Basen</field><field name="mods.name.top">Michael W. W. Adams</field><field name="mods.name.top">Universität Rostock</field><field name="mods.name.top">Universität Rostock. Mathematisch-Naturwissenschaftliche Fakultät</field><field name="mods.author">Laura Sofie Nissen</field><field name="mods.place">Rostock</field><field name="mods.publisher">Universität Rostock</field><field name="mods.genre">epub.dissertation</field><field name="mods.identifier">https://purl.uni-rostock.de/rosdok/id00004885</field><field name="mods.identifier">urn:nbn:de:gbv:28-rosdok_id00004885-1</field><field name="mods.identifier">10.18453/rosdok_id00004885</field><field name="mods.abstract">This study focussed on the versatile AOR from Thermoanaerobacter sp. strain X514 (AORX514), which was biochemically characterized by producing a His-tagged version in Thermoanaerobacter kivui. The function of the enzyme was confirmed, as aldehyde-oxidation activity with the native redox partner ferredoxin, as well as with artificial redox partners. Optimization of the medium did increase specific activity of the heterologous protein, which is active over a wide temperature and pH range, and is able to oxidize a wide variety of aldehydes to their corresponding acids.</field><field name="mods.abstract">Diese Studie konzentrierte sich auf die vielseitige AOR von Thermoanaerobacter sp. Stamm X514 (AORX514), die durch Produktion einer His-markierten Version in Thermoanaerobacter kivui biochemisch charakterisiert wurde. Die Funktion des Enzyms wurde bestätigt, da die Aldehyd-Oxidationsaktivität sowohl mit dem nativen Redoxpartner Ferredoxin als auch mit künstlichen Redoxpartnern nachgewiesen wurde. Optimierung erhöhte die spezifische Aktivität des heterologen Proteins, welches über eine weite Temperatur und pH Spanne aktiv war und eine Vielfalt von Aldehyden zu organischen Säuren oxidierte.</field><field name="mods.dateIssued">2023</field><field name="mods.yearIssued">2023</field><field name="mods.note.referee">Mirko Basen (Institute of Biological Sciences, Universität Rostock) ; Michael W. W. Adams (Department of Biochemistry and Molecular Biology)</field><field name="mods.note.personal_details">[{"name":"Basen, Mirko","affil":"Institute of Biological Sciences, Universität Rostock"},{"name":"Adams, Michael W. W.","affil":"Department of Biochemistry and Molecular Biology"}]</field><field name="mods.note.university_thesis_note">Dissertation, Universität Rostock, 2024</field><field name="mods.note.statement of responsibility">vorgelegt von Laura Sofie Nissen</field><field name="mods.type">epub.dissertation</field><field name="search_result_link_text">1
        Nissen_Dissertation_2025.pdf
        
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        rosdok/id000048851931833745Oau2025-07-252025-07-25T15:22:33ZrdaConverted from PICA to MODS using Pica2MODS XSLT Transformer 2.10 [SCM: "f6c168af690edb7cb65ef34e4a2bf7f8714c5d38" "v2.10" "2024-03-28T14:43:08+0100"] with mode 'DEFAULT'.DissertationHochschulschriftBiochemical characterization of aldehyde:ferredoxin oxidoreductase from the thermophilic bacterium Thermoanaerobacter sp. strain X514This study focussed on the versatile AOR from Thermoanaerobacter sp. strain X514 (AORX514), which was biochemically characterized by producing a His-tagged version in Thermoanaerobacter kivui. The function of the enzyme was confirmed, as aldehyde-oxidation activity with the native redox partner ferredoxin, as well as with artificial redox partners. Optimization of the medium did increase specific activity of the heterologous protein, which is active over a wide temperature and pH range, and is able to oxidize a wide variety of aldehydes to their corresponding acids.Diese Studie konzentrierte sich auf die vielseitige AOR von Thermoanaerobacter sp. Stamm X514 (AORX514), die durch Produktion einer His-markierten Version in Thermoanaerobacter kivui biochemisch charakterisiert wurde. Die Funktion des Enzyms wurde bestätigt, da die Aldehyd-Oxidationsaktivität sowohl mit dem nativen Redoxpartner Ferredoxin als auch mit künstlichen Redoxpartnern nachgewiesen wurde. Optimierung erhöhte die spezifische Aktivität des heterologen Proteins, welches über eine weite Temperatur und pH Spanne aktiv war und eine Vielfalt von Aldehyden zu organischen Säuren oxidierte.Laura SofieNissen1995 -VerfasserInaut1372417885MirkoBasenAkademischeR BetreuerIndgsInstitute of Biological Sciences, Universität RostockMichael W. W.AdamsAkademischeR BetreuerIndgsDepartment of Biochemistry and Molecular Biology38329-6Universität Rostock1419 - 19761990 -Grad-verleihende Institutiondgg2147083-2Universität Rostock. Mathematisch-Naturwissenschaftliche FakultätGrad-verleihende Institutiondgghttps://purl.uni-rostock.de/rosdok/id00004885urn:nbn:de:gbv:28-rosdok_id00004885-110.18453/rosdok_id00004885500 Naturwissenschaften570 Biowissenschaften, BiologieMathematisch-Naturwissenschaftliche Fakultätalle Rechte vorbehaltenNutzungsrechte erteiltLizenz Metadaten: CC0frei zugänglich (Open Access)en2023Universität RostockRostockmonographic202420232025Universitätsbibliothek RostockRostock2025Universitätsbibliothek Rostockhttps://purl.uni-rostock.de/rosdok/id00004885Mirko Basen (Institute of Biological Sciences, Universität Rostock) ; Michael W. W. Adams (Department of Biochemistry and Molecular Biology)[{"name":"Basen, Mirko","affil":"Institute of Biological Sciences, Universität Rostock"},{"name":"Adams, Michael W. W.","affil":"Department of Biochemistry and Molecular Biology"}]Dissertation, Universität Rostock, 2024vorgelegt von Laura Sofie Nissen
              
                Basen, Mirko
                Institute of Biological Sciences, Universität Rostock
              
              
                Adams, Michael W. W.
                Department of Biochemistry and Molecular Biology
              
            
      
    
  
  
    
      2025-07-25T15:04:54.089Z
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      MCRJANITOR</field><field name="derivateLabel">fulltext</field><field name="ir.pdffulltext_url">file/rosdok_disshab_0000003293/rosdok_derivate_0000225137/Nissen_Dissertation_2025.pdf</field><field name="mods.title">Biochemical characterization of aldehyde:ferredoxin oxidoreductase from the thermophilic bacterium Thermoanaerobacter sp. strain X514</field><field name="mods.title.main">Biochemical characterization of aldehyde:ferredoxin oxidoreductase from the thermophilic bacterium Thermoanaerobacter sp. strain X514</field><field name="mods.title.subtitle"></field><field name="mods.nameIdentifier">gnd:1372417885</field><field name="mods.nameIdentifier">gnd:38329-6</field><field name="mods.nameIdentifier">gnd:2147083-2</field><field name="mods.nameIdentifier.top">gnd:1372417885</field><field name="mods.nameIdentifier.top">gnd:38329-6</field><field name="mods.nameIdentifier.top">gnd:2147083-2</field><doc><field name="id">rosdok_disshab_0000003293-d1118548e54</field><field name="mods.nameIdentifier">gnd:1372417885</field><field name="mods.name">Laura Sofie Nissen</field><field name="mods.name.top">Laura Sofie Nissen</field></doc><doc><field name="id">rosdok_disshab_0000003293-d1118548e68</field><field name="mods.name">Mirko Basen</field><field name="mods.name.top">Mirko Basen</field></doc><doc><field name="id">rosdok_disshab_0000003293-d1118548e79</field><field name="mods.name">Michael W. W. Adams</field><field name="mods.name.top">Michael W. W. Adams</field></doc><doc><field name="id">rosdok_disshab_0000003293-d1118548e91</field><field name="mods.nameIdentifier">gnd:38329-6</field><field name="mods.name">Universität Rostock</field><field name="mods.name.top">Universität Rostock</field></doc><doc><field name="id">rosdok_disshab_0000003293-d1118548e104</field><field name="mods.nameIdentifier">gnd:2147083-2</field><field name="mods.name">Universität Rostock. Mathematisch-Naturwissenschaftliche Fakultät</field><field name="mods.name.top">Universität Rostock. Mathematisch-Naturwissenschaftliche Fakultät</field></doc><field name="mods.name">Laura Sofie Nissen</field><field name="mods.name">Mirko Basen</field><field name="mods.name">Michael W. W. Adams</field><field name="mods.name">Universität Rostock</field><field name="mods.name">Universität Rostock. Mathematisch-Naturwissenschaftliche Fakultät</field><field name="mods.name.top">Laura Sofie Nissen</field><field name="mods.name.top">Mirko Basen</field><field name="mods.name.top">Michael W. W. Adams</field><field name="mods.name.top">Universität Rostock</field><field name="mods.name.top">Universität Rostock. Mathematisch-Naturwissenschaftliche Fakultät</field><field name="mods.author">Laura Sofie Nissen</field><field name="mods.place">Rostock</field><field name="mods.publisher">Universität Rostock</field><field name="mods.genre">epub.dissertation</field><field name="mods.identifier">https://purl.uni-rostock.de/rosdok/id00004885</field><field name="mods.identifier">urn:nbn:de:gbv:28-rosdok_id00004885-1</field><field name="mods.identifier">10.18453/rosdok_id00004885</field><field name="mods.abstract">This study focussed on the versatile AOR from Thermoanaerobacter sp. strain X514 (AORX514), which was biochemically characterized by producing a His-tagged version in Thermoanaerobacter kivui. The function of the enzyme was confirmed, as aldehyde-oxidation activity with the native redox partner ferredoxin, as well as with artificial redox partners. Optimization of the medium did increase specific activity of the heterologous protein, which is active over a wide temperature and pH range, and is able to oxidize a wide variety of aldehydes to their corresponding acids.</field><field name="mods.abstract">Diese Studie konzentrierte sich auf die vielseitige AOR von Thermoanaerobacter sp. Stamm X514 (AORX514), die durch Produktion einer His-markierten Version in Thermoanaerobacter kivui biochemisch charakterisiert wurde. Die Funktion des Enzyms wurde bestätigt, da die Aldehyd-Oxidationsaktivität sowohl mit dem nativen Redoxpartner Ferredoxin als auch mit künstlichen Redoxpartnern nachgewiesen wurde. Optimierung erhöhte die spezifische Aktivität des heterologen Proteins, welches über eine weite Temperatur und pH Spanne aktiv war und eine Vielfalt von Aldehyden zu organischen Säuren oxidierte.</field><field name="mods.dateIssued">2023</field><field name="mods.yearIssued">2023</field><field name="mods.note.referee">Mirko Basen (Institute of Biological Sciences, Universität Rostock) ; Michael W. W. Adams (Department of Biochemistry and Molecular Biology)</field><field name="mods.note.personal_details">[{"name":"Basen, Mirko","affil":"Institute of Biological Sciences, Universität Rostock"},{"name":"Adams, Michael W. W.","affil":"Department of Biochemistry and Molecular Biology"}]</field><field name="mods.note.university_thesis_note">Dissertation, Universität Rostock, 2024</field><field name="mods.note.statement of responsibility">vorgelegt von Laura Sofie Nissen</field><field name="ir.identifier">[xslt]Saxon</field><field name="recordIdentifier">rosdok/id00004885</field><field name="purl">https://purl.uni-rostock.de/rosdok/id00004885</field><field name="ppn">1931833745</field><field name="doi">10.18453/rosdok_id00004885</field><field name="urn">urn:nbn:de:gbv:28-rosdok_id00004885-1</field><field name="ir.creator.result">Laura Sofie Nissen</field><field name="ir.creator.sort">Nissen Laura Sofie</field><field name="ir.title.result">Biochemical characterization of aldehyde:ferredoxin oxidoreductase from the thermophilic bacterium Thermoanaerobacter sp. strain X514</field><field name="ir.doctype.result">Dissertation</field><field name="ir.doctype_en.result">doctoral thesis</field><field name="ir.originInfo.result">Universität Rostock, 2023</field><field name="ir.abstract300.result">This study focussed on the versatile AOR from Thermoanaerobacter sp. strain X514 (AORX514), which was biochemically characterized by producing a His-tagged version in Thermoanaerobacter kivui. The function of the enzyme was confirmed, as aldehyde-oxidation activity with the native redox partner…</field><field name="ir.creator_all">Laura Sofie Nissen</field><field name="ir.title_all">Biochemical characterization of aldehyde:ferredoxin oxidoreductase from the thermophilic bacterium Thermoanaerobacter sp. strain X514</field><field name="ir.location_all">Universitätsbibliothek Rostock</field><field name="ir.location_all">https://purl.uni-rostock.de/rosdok/id00004885</field><field name="ir.creator_all">Laura Sofie</field><field name="ir.creator_all">Nissen</field><field name="ir.creator_all">1995 -</field><field name="ir.creator_all"></field><field name="ir.creator_all">VerfasserIn</field><field name="ir.creator_all">aut</field><field name="ir.creator_all">1372417885</field><field name="ir.creator_all">Mirko</field><field name="ir.creator_all">Basen</field><field name="ir.creator_all"></field><field name="ir.creator_all">AkademischeR BetreuerIn</field><field name="ir.creator_all">dgs</field><field name="ir.creator_all">Institute of Biological Sciences, Universität Rostock</field><field name="ir.creator_all">Michael W. W.</field><field name="ir.creator_all">Adams</field><field name="ir.creator_all"></field><field name="ir.creator_all">AkademischeR BetreuerIn</field><field name="ir.creator_all">dgs</field><field name="ir.creator_all">Department of Biochemistry and Molecular Biology</field><field name="ir.creator_all">38329-6</field><field name="ir.creator_all">Universität Rostock</field><field name="ir.creator_all">1419 - 1976</field><field name="ir.creator_all">1990 -</field><field name="ir.creator_all"></field><field name="ir.creator_all">Grad-verleihende Institution</field><field name="ir.creator_all">dgg</field><field name="ir.creator_all">2147083-2</field><field name="ir.creator_all">Universität Rostock. Mathematisch-Naturwissenschaftliche Fakultät</field><field name="ir.creator_all"></field><field name="ir.creator_all">Grad-verleihende Institution</field><field name="ir.creator_all">dgg</field><field name="ir.identifier">[purl]https://purl.uni-rostock.de/rosdok/id00004885</field><field name="ir.identifier">[urn]urn:nbn:de:gbv:28-rosdok_id00004885-1</field><field name="ir.identifier">[doi]10.18453/rosdok_id00004885</field><field name="ir.oai.setspec.open_access">open_access</field><field name="ir.pubyear_start">2023</field><field name="ir.pubyear_end">2023</field><field name="ir.epoch_class.facet">epoch:21th_century</field><field name="ir.language_class.facet">rfc5646:en</field><field name="ir.doctype_class.facet">doctype:epub.dissertation</field><field name="ir.accesscondition_class.facet">accesscondition:openaccess</field><field name="ir.sdnb_class.facet">SDNB:500</field><field name="ir.sdnb_class.facet">SDNB:570</field><field name="ir.institution_class.facet">institution:unirostock.mnf</field><field name="ir.state_class.facet">state:published</field></doc></add>