{"data":[{"id":"10.15488/22581","type":"dois","attributes":{"doi":"10.15488/22581","identifiers":[],"creators":[{"name":"Wegstein, Deborah","affiliation":[],"nameIdentifiers":[]}],"titles":[{"lang":"","title":"Photokatalytische Kaskadenreaktionen: Kopplung von photokatalytischer in-situ Wasserstoffperoxid-Produktion und Biokatalyse mit Peroxygenasen"}],"publisher":"Hannover : Institutionelles Repositorium der Leibniz Universität Hannover","container":{},"publicationYear":2026,"subjects":[{"subject":"500 | Natural sciences \u0026amp; mathematics::540 | Chemistry \u0026amp; allied sciences","lang":"","subjectScheme":"ddc"},{"subject":"Photokatalyse","lang":"ger","subjectScheme":"other"},{"subject":"enantioselektive Enzymkatalyse","lang":"ger","subjectScheme":"other"},{"subject":"Wasserstoffperoxid","lang":"ger","subjectScheme":"other"},{"subject":"Hydroxylierung","lang":"ger","subjectScheme":"other"},{"subject":"Katalysatorensysteme","lang":"ger","subjectScheme":"other"},{"subject":"Photocatalysis","lang":"eng","subjectScheme":"other"},{"subject":"enantioselective enzymatic catalysis","lang":"eng","subjectScheme":"other"},{"subject":"hydrogen per-oxide","lang":"eng","subjectScheme":"other"}],"contributors":[{"name":"Technische Informationsbibliothek (TIB)","contributorType":"DataManager","affiliation":[],"nameIdentifiers":[]},{"name":"Technische Informationsbibliothek (TIB)","contributorType":"HostingInstitution","affiliation":[],"nameIdentifiers":[]},{"name":"Bloh, Jonathan Zacharias","contributorType":"RelatedPerson","affiliation":[],"nameIdentifiers":[]},{"name":"Kara, Selin","contributorType":"RelatedPerson","affiliation":[],"nameIdentifiers":[]}],"dates":[{"date":"2026-10-01","dateType":"Accepted"},{"date":"2026-10-01","dateType":"Available"},{"date":"2026","dateType":"Issued"}],"language":"de","types":{"schemaOrg":"Thesis","resourceTypeGeneral":"Dissertation","citeproc":"thesis","bibtex":"phdthesis","ris":"THES","resourceType":"DoctoralThesis"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rights":"http://creativecommons.org/licenses/by/3.0/de/"},{"rights":"Attribution 3.0 Germany"}],"descriptions":[{"descriptionType":"Abstract","description":"Durch die Verwendung von Enzymen als Katalysatoren in der chemischen Synthese können hochselektive Reaktionsschritte durchgeführt werden, die zu nach-haltigeren Prozessen beitragen können, indem sie Synthesewege verkürzen und optimieren sowie die Menge an Nebenprodukten reduzieren. Oxidoreduktasen (EC 1), eine Klasse von Enzymen, die viele verschiedene Reaktionstypen katalysieren kann, hat großes Anwendungspotenzial in der syntheti-schen organischen Chemie. Die Anwendung dieser Enzyme wird jedoch oft dadurch erschwert, dass komplexe und kostspielige Co-Faktoren benötigt werden. Die unspezifische Peroxygenase aus Agrocybe aegerita (AaeUPO) ist ein besonderes Mitglied dieser Enzymfamilie. Bei der oxidativen Aktivierung unterschiedlicher C-H-Bindungen nutzt sie ausschließlich Wasserstoffperoxid als Co-Substrat, dieses ist leicht zu produzieren und verursacht somit nur geringe Kosten. Da Per-oxygenasen, wie viele Enzyme, in Gegenwart von Wasserstoffperoxid sehr instabil sind, stellt dies ebenfalls ein Hindernis für ihre Verwendung dar. Es bedarf also einer Strategie, um eine optimale Versorgung mit Wasserstoffperoxid sicherzustellen. Eine Option besteht darin, Wasserstoffperoxid direkt zu produzieren, wie etwa durch die photokatalytische Reduktion von molekularem Sauerstoff. Diese Arbeit zielt darauf ab, Photokatalysatoren wie polymeres Kohlenstoffnitrid für die Reaktionskaskade zu testen und die Reaktionsbedingungen zu optimieren. Eine Kombination mit dem durch UV-Licht inaktivierbarem Enzym ist von Inte-resse, da der eingesetze Katalysator durch sichtbares Licht stimuliert werden kann. Um die erhöhten H2O2-Bildungsraten direkt nutzen zu können, wurde auch die Kombination des Photokatalysators mit Co-Katalysatoren wie Gold oder Anth-rachinon geprüft. Dabei erfolgte eine Variation der Reaktionsparameter für die H2O2-Bildung, darunter Lichtintensität, Wellenlänge, pH-Wert, Sauerstoffdurch-flussrate und Co-Katalysatorbeladung. Diese wurden für den Einsatz in der Reak-tionskaskade mit AaeUPO angepasst. Eine immobilisierte Form der AaeUPO wurde ebenfalls verwendet. Die Resultate wurden mit der Anwendung des En-zyms in ungebundener Form verglichen.","lang":"ger"},{"descriptionType":"Abstract","description":"Utilizing enzymes as catalysts in chemical synthesis allows for reaction steps with a high degree of selectivity, which can enhance sustainability by shortening and optimizing synthesis pathways and minimizing by-product formation. Oxidoreductases (EC 1), a category of enzymes capable of catalyzing various reactions, hold significant promise for use in synthetic organic chemistry. However, the need for complex and costly cofactors often hinders the use of these enzymes. AaeUPO, the unspecific peroxygenase derived from Agrocybe aegerita, is a unique member of this enzyme family. It utilizes solely hydrogen peroxide as a co-substrate for the oxidative activation of different C-H bonds, which is easily produced and thus low-cost. Due to the fact that peroxigenases, similar to many enzymes, are highly unstable when hydrogen peroxide is present, this creates a barrier to their application. Thus, it is necessary to develop a strategy that will guarantee the best possible supply of hydrogen peroxide. A potential option is to create hydrogen peroxide directly, such as via the photocatalytic reduction of molecular oxygen. This work aims to test photocatalysts such as polymeric carbon nitride for the reaction cascade and to optimize the reaction conditions. A combination with the enzyme, which is inactivated by UV light, is interesting as this catalyst can be stimulated by visible light. In order to be able to use the increased H2O2 formation rates directly, the combination of the photocatalyst with co-catalysts such as gold or anthraquinone was also tested. The reaction parameters for H2O2 formation were varied, including light intensity, wavelength, pH value, oxygen flow rate and co- catalyst loading. These were adapted for use in the reaction cascade with AaeUPO. Finally, an immobilized form of AaeUPO was also used. The results were compared with the use of the enzyme in unbound form.","lang":"eng"}],"geoLocations":[],"fundingReferences":[],"url":"https://repo.uni-hannover.de/handle/123456789/22768","contentUrl":null,"metadataVersion":0,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2026-10-07T09:19:06Z","registered":"2026-10-07T09:55:48Z","published":null,"updated":"2026-10-07T10:00:50Z"},"relationships":{"client":{"data":{"id":"tib.luhrepo","type":"clients"}}}},{"id":"10.15488/20544","type":"dois","attributes":{"doi":"10.15488/20544","identifiers":[],"creators":[{"name":"De Santis, Piera","affiliation":[],"nameIdentifiers":[]},{"name":"Petrovai, Noémi","affiliation":[],"nameIdentifiers":[]},{"name":"Meyer, Lars-Erik","affiliation":[],"nameIdentifiers":[]},{"name":"Hobisch, Markus","affiliation":[],"nameIdentifiers":[]},{"name":"Kara, Selin","affiliation":[],"nameIdentifiers":[]}],"titles":[{"lang":"eng","title":"A holistic carrier-bound immobilization approach for unspecific peroxygenase"}],"publisher":"Lausanne : Frontiers Media","container":{},"publicationYear":2022,"subjects":[{"subject":"540","lang":"","subjectScheme":"ddc"},{"subject":"biocatalysis","lang":"eng","subjectScheme":"other"},{"subject":"enzyme stability","lang":"eng","subjectScheme":"other"},{"subject":"immobilization techniques","lang":"eng","subjectScheme":"other"},{"subject":"process intensification","lang":"eng","subjectScheme":"other"},{"subject":"unspecific peroxygenase","lang":"eng","subjectScheme":"other"}],"contributors":[{"name":"Technische Informationsbibliothek (TIB)","contributorType":"DataManager","affiliation":[],"nameIdentifiers":[]},{"name":"Technische Informationsbibliothek (TIB)","contributorType":"HostingInstitution","affiliation":[],"nameIdentifiers":[]}],"dates":[{"date":"2026-02-04","dateType":"Accepted"},{"date":"2026-02-04","dateType":"Available"},{"date":"2022","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"JournalArticle","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Article"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","rightsIdentifier":"cc-by-4.0"},{"rights":"CC BY 4.0 International"}],"descriptions":[{"descriptionType":"Abstract","description":"Unspecific peroxygenases (UPOs) are among the most studied enzymes in the last decade and their well-deserved fame owes to the enzyme’s ability of catalyzing the regio- and stereospecific hydroxylation of non-activated C–H bonds at the only expense of H2O2. This leads to more direct routes for the synthesis of different chiral compounds as well as to easier oxyfunctionalization of complex molecules. Unfortunately, due to the high sensitivity towards the process conditions, UPOs’ application at industrial level has been hampered until now. However, this challenge can be overcome by enzyme immobilization, a valid strategy that has been proven to give several benefits. Within this article, we present three different immobilization procedures suitable for UPOs and two of them led to very promising results. The immobilized enzyme, indeed, shows longer stability and increased robustness to reaction conditions. The immobilized enzyme half-life time is 15-fold higher than for the free AaeUPO PaDa-I and no enzyme deactivation occurred when incubated in organic media for 120 h. Moreover, AaeUPO PaDa-I is proved to be recycled and reused up to 7 times when immobilized.","lang":"eng"}],"geoLocations":[],"fundingReferences":[],"url":"https://repo.uni-hannover.de/handle/123456789/20695","contentUrl":null,"metadataVersion":1,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2026-02-04T15:00:14Z","registered":"2026-02-04T15:00:42Z","published":null,"updated":"2026-10-07T07:55:37Z"},"relationships":{"client":{"data":{"id":"tib.luhrepo","type":"clients"}}}},{"id":"10.15468/nvjndg","type":"dois","attributes":{"doi":"10.15468/nvjndg","identifiers":[{"identifier":"e98a6f16-e32e-44e6-b1e2-821d2f5d8fb6","identifierType":"UUID"}],"creators":[{"name":"Roselyne Ferrari","affiliation":[],"nameIdentifiers":[]},{"name":"Valérie Gautier","affiliation":[],"nameIdentifiers":[]},{"name":"Narumon Tangthirasunun","affiliation":[],"nameIdentifiers":[]},{"name":"Laetitia Chan Ho Tong","affiliation":[],"nameIdentifiers":[]},{"name":"Philippe Silar","affiliation":[],"nameIdentifiers":[]}],"titles":[{"title":"Characterization of the Podospora anserina (Rabenh.) Niessl peroxidase gene family"}],"publisher":"Cryptogamie, Mycologie","container":{},"publicationYear":2024,"subjects":[{"subject":"ne montre pas de modification importante de celle-ci"},{"subject":"suggérant des compensations entre les différents"}],"contributors":[{"name":"Guido Sautter","contributorType":"RelatedPerson","affiliation":[],"nameIdentifiers":[]},{"affiliation":["Plazi"],"name":"plazi","contributorType":"DataCurator","nameIdentifiers":[]}],"dates":[{"date":"2024-02-19","dateType":"Created"},{"date":"2026-09-30","dateType":"Updated"}],"language":"en","types":{"schemaOrg":"Dataset","resourceTypeGeneral":"Dataset","citeproc":"dataset","bibtex":"misc","ris":"DATA","resourceType":"CHECKLIST"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/publicdomain/zero/1.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Zero v1.0 Universal","rightsIdentifier":"cc0-1.0"}],"descriptions":[{"descriptionType":"Abstract","description":"This dataset contains the digitized treatments in Plazi based on the original journal article Ferrari, Roselyne, Gautier, Valérie, Tangthirasunun, Narumon, Tong, Laetitia Chan Ho, Silar, Philippe (2024): Characterization of the Podospora anserina (Rabenh.) Niessl peroxidase gene family. Cryptogamie, Mycologie 45 (2): 11-28, DOI: 10.5252/cryptogamiemycologie2024v45a2, URL: https://sciencepress.mnhn.fr/sites/default/files/articles/pdf/mycologie2024v45a2.pdfABSTRACTMajor role of peroxidases in plant biomass degradation is well-established in the white rot basidiomycetes. On the contrary, peroxidases are not used for this purpose by brown rot basidiomycetes, which use instead a non-enzymatic mechanism. In the case of the ascomycetes, not much is known although these fungi have peroxidase genes. Here, we identify and characterize the peroxidase genes of Podospora anserina (Rabenh.) Niessl, an ascomycete used to study development and lignocellulose degradation. We show that this fungus has one class II peroxidase, one hybrid B peroxidase, one haloperoxidase, four functional aromatic peroxygenases, one glutathione peroxidase, one cytochrome C peroxidase and one alkyl peroxidase, but lacks a dye peroxidase. We show that potentially secreted peroxidases (i.e., the class II, hybrid B, haloperoxidase and aromatic peroxygenase peroxidases) present a patchy phylogenetic distribution compatible with an accessory role in finely adapting the different fungal species to their ecological niche, rather than being involved in fundamental roles in fungal biology. Accordingly, targeted gene deletions of the different P. anserina peroxidase genes identified only one phenotype, seemingly an alteration of the timing of ascospore maturation at intermediate concentration of vanillic acid. However, direct measure of peroxidase activity did not show drastic loss of activity in the tested mutants, suggesting compensation between the enzymes. Hence, in P. anserina, peroxidases appear to have a minor role in biomass degradation, unlike what has been described in white rot fungi, and in this regard P. anserina appears to be similar to brown rot fungi."}],"geoLocations":[],"fundingReferences":[],"url":"https://www.gbif.org/dataset/e98a6f16-e32e-44e6-b1e2-821d2f5d8fb6","contentUrl":null,"metadataVersion":9,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"api","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2024-02-19T14:21:52Z","registered":"2024-02-19T14:21:52Z","published":null,"updated":"2026-09-30T14:47:44Z"},"relationships":{"client":{"data":{"id":"gbif.gbif","type":"clients"}}}},{"id":"10.25673/125567","type":"dois","attributes":{"doi":"10.25673/125567","identifiers":[{"identifier":"1985165406","identifierType":"ppn"}],"creators":[{"name":"Last, Simon","affiliation":[],"nameIdentifiers":[]},{"name":"Gazizova, Alina","affiliation":[],"nameIdentifiers":[]},{"name":"Wittmann, Katharina","affiliation":[],"nameIdentifiers":[]},{"name":"Dietz, Niklas","affiliation":[],"nameIdentifiers":[]},{"name":"Weissenborn, Martin J.","affiliation":[],"nameIdentifiers":[]},{"name":"Langermann und Erlencamp, Jan","affiliation":[],"nameIdentifiers":[]}],"titles":[{"title":"Unspecific peroxygenase-based chemo-enzymatic synthesis of amino alcohols for pharmaceutical preparation"}],"publisher":"Universitäts- und Landesbibliothek Sachsen-Anhalt","container":{},"publicationYear":2026,"subjects":[{"subject":"540","subjectScheme":"ddc"}],"contributors":[{"name":"Universitäts- und Landesbibliothek Sachsen-Anhalt","contributorType":"DataManager","affiliation":[],"nameIdentifiers":[]},{"name":"Martin-Luther Universität","contributorType":"HostingInstitution","affiliation":[],"nameIdentifiers":[]}],"dates":[{"date":"2026-09-28","dateType":"Accepted"},{"date":"2026-09-28","dateType":"Available"},{"date":"2026","dateType":"Issued"}],"language":null,"types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"Text","citeproc":"article-journal","bibtex":"article","ris":"RPRT","resourceType":"Article"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","rightsIdentifier":"cc-by-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"This study explores the use of unspecific peroxygenases for the enantioselective preparation of amino alcohol-based pharmaceuticals and their respective precursors. The aim of this work was to develop a practical concept by simplifying the otherwise complex synthesis approach, thereby expanding the application of unspecific peroxygenases toward chemo-enzymatic synthesis. To introduce hydroxy groups at specific positions within protected amines, the unspecific peroxygenase (UPO) was used, which facilitated the enantioselective synthesis toward shorter overall reaction pathways and thus may serve as an addition to the preparative toolbox with this type of enzyme."}],"geoLocations":[],"fundingReferences":[],"url":"https://opendata.uni-halle.de//handle/1981185920/127502","contentUrl":null,"metadataVersion":0,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2026-09-28T20:00:11Z","registered":"2026-09-28T20:00:41Z","published":null,"updated":"2026-09-29T20:00:14Z"},"relationships":{"client":{"data":{"id":"zbmed.ulbhalle","type":"clients"}}}},{"id":"10.15488/15392","type":"dois","attributes":{"doi":"10.15488/15392","identifiers":[{"identifier":"De Santis, P.; Wegstein, D.; Burek, B.O.; Patzsch, J.; Alcalde, M. et al.: Robust Light Driven Enzymatic Oxyfunctionalization via Immobilization of Unspecific Peroxygenase. In: ChemSusChem 16 (2023), Nr. 23, e202300613. DOI: https://doi.org/10.1002/cssc.202300613","identifierType":"citation"},{"identifier":"https://repo.uni-hannover.de/handle/123456789/15512","identifierType":"uri"}],"creators":[{"name":"De Santis, Piera","affiliation":[],"nameIdentifiers":[]},{"name":"Wegstein, Deborah","affiliation":[],"nameIdentifiers":[]},{"name":"Burek, Bastien O.","affiliation":[],"nameIdentifiers":[]},{"name":"Patzsch, Jacqueline","affiliation":[],"nameIdentifiers":[]},{"name":"Alcalde, Miguel","affiliation":[],"nameIdentifiers":[]},{"name":"Kroutil, Wolfgang","affiliation":[],"nameIdentifiers":[]},{"name":"Bloh, Jonathan Z.","affiliation":[],"nameIdentifiers":[]},{"name":"Kara, Selin","affiliation":[],"nameIdentifiers":[]}],"titles":[{"lang":"eng","title":"Robust Light Driven Enzymatic Oxyfunctionalization via Immobilization of Unspecific Peroxygenase"}],"publisher":"Weinheim : Wiley-VCH","container":{},"publicationYear":2023,"subjects":[{"subject":"500 | Naturwissenschaften::540 | Chemie","lang":"de","subjectScheme":"ddc"},{"subject":"biocatalysis","lang":"eng","subjectScheme":"other"},{"subject":"g-C N 3 4","lang":"eng","subjectScheme":"other"},{"subject":"immobilized enzyme","lang":"eng","subjectScheme":"other"},{"subject":"peroxygenases","lang":"eng","subjectScheme":"other"},{"subject":"photocatalysis","lang":"eng","subjectScheme":"other"}],"contributors":[{"name":"Technische Informationsbibliothek (TIB)","contributorType":"DataManager","affiliation":[],"nameIdentifiers":[]},{"name":"Technische Informationsbibliothek (TIB)","contributorType":"HostingInstitution","affiliation":[],"nameIdentifiers":[]}],"dates":[{"date":"2023-11-21","dateType":"Accepted"},{"date":"2023-11-21","dateType":"Available"},{"date":"2023","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"JournalArticle","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Article"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution Non Commercial 4.0 International","rightsIdentifier":"cc-by-nc-4.0"},{"rights":"CC BY-NC 4.0 International"}],"descriptions":[{"descriptionType":"Abstract","description":"Unspecific peroxygenases have attracted interest in synthetic chemistry, especially for the oxidative activation of C−H bonds, as they only require hydrogen peroxide (H2O2) instead of a cofactor. Due to their instability in even small amounts of H2O2, different strategies like enzyme immobilization or in situ H2O2 production have been developed to improve the stability of these enzymes. While most strategies have been studied separately, a combination of photocatalysis with immobilized enzymes was only recently reported. To show the advantages and limiting factors of immobilized enzyme in a photobiocatalytic reaction, a comparison is made between free and immobilized enzymes. Adjustment of critical parameters such as (i) enzyme and substrate concentration, (ii) illumination wavelength and (iii) light intensity results in significantly increased enzyme stabilities of the immobilized variant. Moreover, under optimized conditions a turnover number of 334,500 was reached.","lang":"eng"}],"geoLocations":[],"fundingReferences":[],"url":"https://www.repo.uni-hannover.de/handle/123456789/15512","contentUrl":null,"metadataVersion":3,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2023-11-21T05:45:20Z","registered":"2023-11-21T06:15:11Z","published":null,"updated":"2026-09-25T13:00:35Z"},"relationships":{"client":{"data":{"id":"tib.luhrepo","type":"clients"}}}},{"id":"10.5281/zenodo.10679618","type":"dois","attributes":{"doi":"10.5281/zenodo.10679618","identifiers":[{"identifier":"http://treatment.plazi.org/id/038387E2323B4D7C2874FA6378D8F85A","identifierType":"URL"}],"creators":[{"nameType":"Personal","affiliation":["Université Paris Diderot, Sorbonne Paris Cité, Laboratoire Interdisciplinaire des Énergies de Demain, 75205 Paris Cité Cedex 13 (France)"],"givenName":"Roselyne","familyName":"Ferrari","name":"Ferrari, Roselyne","nameIdentifiers":[]},{"nameType":"Personal","affiliation":["Université Paris Diderot, Sorbonne Paris Cité, Laboratoire Interdisciplinaire des Énergies de Demain, 75205 Paris Cité Cedex 13 (France)"],"givenName":"Valérie","familyName":"Gautier","name":"Gautier, Valérie","nameIdentifiers":[]},{"nameType":"Personal","affiliation":["Department of Biology, Faculty of Science, King Mongkut's Institute of Technology Ladkrabang, Bangkok, 10520 (Thailand) Université Paris Diderot, Sorbonne Paris Cité, Laboratoire Interdisciplinaire des Énergies de Demain, 75205 Paris Cité Cedex 13 (France) philippe. silar @ univ-paris-diderot. fr (corresponding author)"],"givenName":"Narumon","familyName":"Tangthirasunun","name":"Tangthirasunun, Narumon","nameIdentifiers":[]},{"nameType":"Personal","affiliation":["Université Paris Diderot, Sorbonne Paris Cité, Laboratoire Interdisciplinaire des Énergies de Demain, 75205 Paris Cité Cedex 13 (France)"],"givenName":"Laetitia Chan Ho","familyName":"Tong","name":"Tong, Laetitia Chan Ho","nameIdentifiers":[]},{"nameType":"Personal","affiliation":["Université Paris Diderot, Sorbonne Paris Cité, Laboratoire Interdisciplinaire des Énergies de Demain, 75205 Paris Cité Cedex 13 (France)"],"givenName":"Philippe","familyName":"Silar","name":"Silar, Philippe","nameIdentifiers":[]}],"titles":[{"title":"Podospora anserina Niessl"}],"publisher":"Zenodo","container":{},"publicationYear":2024,"subjects":[{"subject":"Biodiversity"},{"subject":"Taxonomy"},{"subject":"Fungi"},{"subject":"Ascomycota"},{"subject":"Sordariomycetes"},{"subject":"Sordariales"},{"subject":"Lasiosphaeriaceae"},{"subject":"Podospora"},{"subject":"Podospora anserina"}],"contributors":[],"dates":[{"date":"2024-02-15","dateType":"Issued"}],"language":null,"types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"Text","citeproc":"article-journal","bibtex":"article","ris":"RPRT","resourceType":"Taxonomic treatment"},"relatedIdentifiers":[{"relationType":"IsPartOf","resourceTypeGeneral":"JournalArticle","relatedIdentifier":"10.5252/cryptogamiemycologie2024v45a2","relatedIdentifierType":"DOI"},{"relationType":"IsPartOf","resourceTypeGeneral":"JournalArticle","relatedIdentifier":"http://zenodo.org/record/10679599","relatedIdentifierType":"URL"},{"relationType":"IsPartOf","resourceTypeGeneral":"JournalArticle","relatedIdentifier":"http://publication.plazi.org/id/FFBAFF9A32304D772B59FFB07C2FFFB1","relatedIdentifierType":"URL"},{"relationType":"IsSourceOf","relatedIdentifier":"https://biodiversitypmc.sibils.org/collections/plazi/038387E2323B4D7C2874FA6378D8F85A","relatedIdentifierType":"URL"},{"relationType":"IsSourceOf","relatedIdentifier":"https://www.gbif.org/species/221339017","relatedIdentifierType":"URL"},{"relationType":"IsSourceOf","relatedIdentifier":"https://www.checklistbank.org/dataset/288671/taxon/038387E2323B4D7C2874FA6378D8F85A.taxon","relatedIdentifierType":"URL"},{"relationType":"Cites","resourceTypeGeneral":"Dataset","relatedIdentifier":"10.5281/zenodo.15155937","relatedIdentifierType":"DOI"},{"relationType":"Cites","resourceTypeGeneral":"Dataset","relatedIdentifier":"http://table.plazi.org/id/DF55667C32354D722BDAFF6B7FC7FEB5","relatedIdentifierType":"URL"},{"relationType":"HasVersion","relatedIdentifier":"10.5281/zenodo.10679619","relatedIdentifierType":"DOI"}],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/publicdomain/zero/1.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Zero v1.0 Universal","rightsIdentifier":"cc0-1.0"}],"descriptions":[{"descriptionType":"Abstract","description":"EXPRESSION OF PEROXIDASE GENES IN P. ANSERINA MYCELIUM\nWe evaluated the expression of peroxidase genes during two days and four days of growth on M2 medium (Table 1), by analyzing microarrays and RNAseq data generated in previous studies (Bidard et al. 2012; Silar et al. 2019) (Table 1). We could evidence expression of all peroxidase genes (except for the “ Pa_2_10 ” pseudogene). The hybrid B peroxidase Pa_2_9370 and the aromatic peroxygenase Pa_0_370 genes were highly transcribed; on the contrary, the class II peroxidase Pa_1_5970 and the aromatic peroxygenase Pa_5_12205 gene were poorly expressed, a feature compatible with the lack of the aromatic peroxygenase Pa_5_ 1220 in secretomes data. Note that analysis of RNAseq data from perithecia showed that the class II peroxidase Pa_1_5970 gene was much more transcribed in these sexual fruiting bodies than in the mycelium, especially in four-day-old perithecia."},{"descriptionType":"Other","description":"Published as part of Ferrari, Roselyne, Gautier, Valérie, Tangthirasunun, Narumon, Tong, Laetitia Chan Ho \u0026 Silar, Philippe, 2024, Characterization of the Podospora anserina (Rabenh.) Niessl peroxidase gene family, pp. 11-28 in Cryptogamie, Mycologie 45 (2) on page 20, DOI: 10.5252/cryptogamiemycologie2024v45a2, http://zenodo.org/record/10679599"}],"geoLocations":[],"fundingReferences":[],"url":"https://zenodo.org/doi/10.5281/zenodo.10679618","contentUrl":null,"metadataVersion":8,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"api","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":1,"citationCount":0,"partCount":0,"partOfCount":1,"versionCount":2,"versionOfCount":1,"created":"2024-02-19T14:17:46Z","registered":"2024-02-19T14:17:46Z","published":null,"updated":"2026-09-21T21:55:01Z"},"relationships":{"client":{"data":{"id":"cern.zenodo","type":"clients"}}}},{"id":"10.5281/zenodo.10679619","type":"dois","attributes":{"doi":"10.5281/zenodo.10679619","identifiers":[{"identifier":"oai:zenodo.org:10679619","identifierType":"oai"},{"identifier":"http://treatment.plazi.org/id/038387E2323B4D7C2874FA6378D8F85A","identifierType":"URL"}],"creators":[{"nameType":"Personal","affiliation":["Université Paris Diderot, Sorbonne Paris Cité, Laboratoire Interdisciplinaire des Énergies de Demain, 75205 Paris Cité Cedex 13 (France)"],"givenName":"Roselyne","familyName":"Ferrari","name":"Ferrari, Roselyne","nameIdentifiers":[]},{"nameType":"Personal","affiliation":["Université Paris Diderot, Sorbonne Paris Cité, Laboratoire Interdisciplinaire des Énergies de Demain, 75205 Paris Cité Cedex 13 (France)"],"givenName":"Valérie","familyName":"Gautier","name":"Gautier, Valérie","nameIdentifiers":[]},{"nameType":"Personal","affiliation":["Department of Biology, Faculty of Science, King Mongkut's Institute of Technology Ladkrabang, Bangkok, 10520 (Thailand) Université Paris Diderot, Sorbonne Paris Cité, Laboratoire Interdisciplinaire des Énergies de Demain, 75205 Paris Cité Cedex 13 (France) philippe. silar @ univ-paris-diderot. fr (corresponding author)"],"givenName":"Narumon","familyName":"Tangthirasunun","name":"Tangthirasunun, Narumon","nameIdentifiers":[]},{"nameType":"Personal","affiliation":["Université Paris Diderot, Sorbonne Paris Cité, Laboratoire Interdisciplinaire des Énergies de Demain, 75205 Paris Cité Cedex 13 (France)"],"givenName":"Laetitia Chan Ho","familyName":"Tong","name":"Tong, Laetitia Chan Ho","nameIdentifiers":[]},{"nameType":"Personal","affiliation":["Université Paris Diderot, Sorbonne Paris Cité, Laboratoire Interdisciplinaire des Énergies de Demain, 75205 Paris Cité Cedex 13 (France)"],"givenName":"Philippe","familyName":"Silar","name":"Silar, Philippe","nameIdentifiers":[]}],"titles":[{"title":"Podospora anserina Niessl"}],"publisher":"Zenodo","container":{},"publicationYear":2024,"subjects":[{"subject":"Biodiversity"},{"subject":"Taxonomy"},{"subject":"Fungi"},{"subject":"Ascomycota"},{"subject":"Sordariomycetes"},{"subject":"Sordariales"},{"subject":"Lasiosphaeriaceae"},{"subject":"Podospora"},{"subject":"Podospora anserina"}],"contributors":[],"dates":[{"date":"2024-02-15","dateType":"Issued"}],"language":null,"types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"Text","citeproc":"article-journal","bibtex":"article","ris":"RPRT","resourceType":"Taxonomic treatment"},"relatedIdentifiers":[{"relationType":"IsPartOf","resourceTypeGeneral":"JournalArticle","relatedIdentifier":"10.5252/cryptogamiemycologie2024v45a2","relatedIdentifierType":"DOI"},{"relationType":"IsPartOf","resourceTypeGeneral":"JournalArticle","relatedIdentifier":"http://zenodo.org/record/10679599","relatedIdentifierType":"URL"},{"relationType":"IsPartOf","resourceTypeGeneral":"JournalArticle","relatedIdentifier":"http://publication.plazi.org/id/FFBAFF9A32304D772B59FFB07C2FFFB1","relatedIdentifierType":"URL"},{"relationType":"IsSourceOf","relatedIdentifier":"https://biodiversitypmc.sibils.org/collections/plazi/038387E2323B4D7C2874FA6378D8F85A","relatedIdentifierType":"URL"},{"relationType":"IsSourceOf","relatedIdentifier":"https://www.gbif.org/species/221339017","relatedIdentifierType":"URL"},{"relationType":"IsSourceOf","relatedIdentifier":"https://www.checklistbank.org/dataset/288671/taxon/038387E2323B4D7C2874FA6378D8F85A.taxon","relatedIdentifierType":"URL"},{"relationType":"Cites","resourceTypeGeneral":"Dataset","relatedIdentifier":"10.5281/zenodo.15155937","relatedIdentifierType":"DOI"},{"relationType":"Cites","resourceTypeGeneral":"Dataset","relatedIdentifier":"http://table.plazi.org/id/DF55667C32354D722BDAFF6B7FC7FEB5","relatedIdentifierType":"URL"},{"relationType":"IsVersionOf","relatedIdentifier":"10.5281/zenodo.10679618","relatedIdentifierType":"DOI"}],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/publicdomain/zero/1.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Zero v1.0 Universal","rightsIdentifier":"cc0-1.0"}],"descriptions":[{"descriptionType":"Abstract","description":"EXPRESSION OF PEROXIDASE GENES IN P. ANSERINA MYCELIUM\nWe evaluated the expression of peroxidase genes during two days and four days of growth on M2 medium (Table 1), by analyzing microarrays and RNAseq data generated in previous studies (Bidard et al. 2012; Silar et al. 2019) (Table 1). We could evidence expression of all peroxidase genes (except for the “ Pa_2_10 ” pseudogene). The hybrid B peroxidase Pa_2_9370 and the aromatic peroxygenase Pa_0_370 genes were highly transcribed; on the contrary, the class II peroxidase Pa_1_5970 and the aromatic peroxygenase Pa_5_12205 gene were poorly expressed, a feature compatible with the lack of the aromatic peroxygenase Pa_5_ 1220 in secretomes data. Note that analysis of RNAseq data from perithecia showed that the class II peroxidase Pa_1_5970 gene was much more transcribed in these sexual fruiting bodies than in the mycelium, especially in four-day-old perithecia."},{"descriptionType":"Other","description":"Published as part of Ferrari, Roselyne, Gautier, Valérie, Tangthirasunun, Narumon, Tong, Laetitia Chan Ho \u0026 Silar, Philippe, 2024, Characterization of the Podospora anserina (Rabenh.) Niessl peroxidase gene family, pp. 11-28 in Cryptogamie, Mycologie 45 (2) on page 20, DOI: 10.5252/cryptogamiemycologie2024v45a2, http://zenodo.org/record/10679599"}],"geoLocations":[],"fundingReferences":[],"url":"https://zenodo.org/doi/10.5281/zenodo.10679619","contentUrl":null,"metadataVersion":7,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"api","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":2,"citationCount":0,"partCount":0,"partOfCount":1,"versionCount":0,"versionOfCount":1,"created":"2024-02-19T14:17:46Z","registered":"2024-02-19T14:17:46Z","published":null,"updated":"2026-09-21T21:55:01Z"},"relationships":{"client":{"data":{"id":"cern.zenodo","type":"clients"}}}},{"id":"10.5445/ir/1000196868","type":"dois","attributes":{"doi":"10.5445/ir/1000196868","identifiers":[],"creators":[{"name":"Dirks, Tim","affiliation":[],"nameIdentifiers":[]},{"name":"Maya, Mery Sheryll Hernandez","affiliation":[],"nameIdentifiers":[]},{"name":"Stoesser, Davina","affiliation":[],"nameIdentifiers":[]},{"name":"Tille, Sophia","affiliation":[],"nameIdentifiers":[]},{"name":"Hollmann, Frank","affiliation":[],"nameIdentifiers":[]},{"name":"Munoz, Alexander Navarrete","affiliation":[],"nameIdentifiers":[]}],"titles":[{"title":"Nanosecond Pulsed Microwave Plasma Torch for Continuous In‐Line H$_2$O$_2$ Supply: A Path to Stable and Scalable Plasma‐Driven Biocatalysis"}],"publisher":"Wiley-VCH Verlag","container":{},"publicationYear":2026,"subjects":[{"subject":"hydroxylation"},{"subject":"immobilization"},{"subject":"microwave plasma"},{"subject":"peroxygenase"},{"subject":"tandem plasma-biocatalysis"}],"contributors":[],"dates":[],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"Text","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Journal Article"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsUri":"info:eu-repo/semantics/openAccess","rights":"Open Access"},{"rightsUri":"https://creativecommons.org/licenses/by/4.0/deed.de","rights":"Creative Commons Namensnennung 4.0 International"}],"descriptions":[{"descriptionType":"Abstract","description":"Plasma-driven H$_2$O$_2$ generation offers a potential sustainable route for biotransformations, but its application is hindered by challenges such as insufficient H$_2$O$_2$ production and enzyme degradation. This study establishes plasma-driven biocatalysis using a nanosecond pulsed microwave plasma torch (npMWPT), highlighting its unique advantages over previously applied sources. npMWPT-driven biocatalysis addresses insufficient plasma-generated H$_2$O$_2$ production by enabling continuous H$_2$O$_2$ supply while decoupling plasma treatment from enzymatic reactions. We investigated the effectiveness of npMWPT-driven biocatalysis using both immobilized and free recombinant unspecific peroxygenase from Agrocybe aegerita (rAaeUPO) to convert ABTS and ethylbenzene. For ABTS, immobilized rAaeUPO demonstrated reusability across five reaction cycles (turnover number TON 44,637 µmol$_{ABTS*}$ µmoL$^{−1}$$_{rAaeUPO}$). The decoupling of npMWPT-based H$_2$O$_2$ production resulted in a TON of 66,495 µmol$_{(R)-1-PhOl}$ µmoL$^{−1}$$_{rAaeUPO}$ with ethylbenzene for free rAaeUPO, outperforming the use of immobilized rAaeUPO for the first time in plasma-driven biocatalysis (TTN 22,116). Mixing optimization improved conversion rates, while observed enzyme inactivation under continuous operation revealed that H$_2$O$_2$ generation exceeded enzymatic consumption under the investigated conditions. The present study identifies supply-demand matching as the key optimization target for npMWPT-driven biocatalysis. This proof-of-principle work demonstrates the successful integration of spatially decoupled npMWPT H$_2$O$_2$ generation with peroxygenase-based biocatalysis and provides a basis for future process-controlled plasma-driven biocatalysis."}],"geoLocations":[],"fundingReferences":[],"url":"https://publikationen.bibliothek.kit.edu/1000196868","contentUrl":null,"metadataVersion":0,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2026-09-08T06:23:54Z","registered":"2026-09-08T06:23:55Z","published":null,"updated":"2026-09-08T06:23:55Z"},"relationships":{"client":{"data":{"id":"tib.kit","type":"clients"}}}},{"id":"10.48350/31603","type":"dois","attributes":{"doi":"10.48350/31603","identifiers":[{"identifier":"https://boris-portal.unibe.ch/handle/20.500.12422/105051","identifierType":"URL"}],"creators":[{"name":"Kluge, Martin","affiliation":[],"nameIdentifiers":[]},{"name":"Ullrich, René","affiliation":[],"nameIdentifiers":[]},{"name":"Dolge, Christoph","affiliation":[],"nameIdentifiers":[]},{"affiliation":["University Clinic for Obstetrics and Gynecology"],"name":"Scheibner, Katrin","nameIdentifiers":[]}],"titles":[{"title":"Hydroxylation of naphthalene by aromatic peroxygenase from Agrocybe aegerita proceeds via oxygen transfer from H2O2 and intermediary epoxidation"}],"publisher":"University of Bern","container":{},"publicationYear":2009,"subjects":[],"contributors":[],"dates":[{"date":"2009","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"JournalArticle","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Text"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsUri":"http://purl.org/coar/access_right/c_abf2","rights":"open.access"}],"descriptions":[{"descriptionType":"Abstract","description":"Agrocybe aegerita peroxidase/peroxygenase (AaP) is an extracellular fungal biocatalyst that selectively hydroxylates the aromatic ring of naphthalene. Under alkaline conditions, the reaction proceeds via the formation of an intermediary product with a molecular mass of 144 and a characteristic UV absorption spectrum (A(max) 210, 267, and 303 nm). The compound was semistable at pH 9 but spontaneously hydrolyzed under acidic conditions (pH\u0026lt;7) into 1-naphthol as major product and traces of 2-naphthol. Based on these findings and literature data, we propose naphthalene 1,2-oxide as the primary product of AaP-catalyzed oxygenation of naphthalene. Using (18)O-labeled hydrogen peroxide, the origin of the oxygen atom transferred to naphthalene was proved to be the peroxide that acts both as oxidant (primary electron acceptor) and oxygen source."}],"geoLocations":[],"fundingReferences":[],"url":"https://boris-portal.unibe.ch/entities/publication/49695bce-dddd-43d0-a520-4e14bb0d6b07","contentUrl":null,"metadataVersion":6,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2022-03-10T15:41:44Z","registered":"2022-03-10T15:41:50Z","published":null,"updated":"2026-09-08T03:58:27Z"},"relationships":{"client":{"data":{"id":"unibe.boris-portal","type":"clients"}}}},{"id":"10.48350/31601","type":"dois","attributes":{"doi":"10.48350/31601","identifiers":[{"identifier":"https://boris-portal.unibe.ch/handle/20.500.12422/105049","identifierType":"URL"}],"creators":[{"name":"Pecyna, Marek J","affiliation":[],"nameIdentifiers":[]},{"name":"Ullrich, René","affiliation":[],"nameIdentifiers":[]},{"name":"Bittner, Britta","affiliation":[],"nameIdentifiers":[]},{"name":"Clemens, André","affiliation":[],"nameIdentifiers":[]},{"affiliation":["University Clinic for Obstetrics and Gynecology"],"name":"Scheibner, Katrin","nameIdentifiers":[]},{"name":"Hofrichter, Martin","affiliation":[],"nameIdentifiers":[]}],"titles":[{"title":"Molecular characterization of aromatic peroxygenase from Agrocybe aegerita"}],"publisher":"University of Bern","container":{},"publicationYear":2009,"subjects":[],"contributors":[],"dates":[{"date":"2009","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"JournalArticle","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Text"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsUri":"http://purl.org/coar/access_right/c_abf2","rights":"open.access"}],"descriptions":[{"descriptionType":"Abstract","description":"Recently, a novel group of fungal peroxidases, known as the aromatic peroxygenases (APO), has been discovered. Members of these extracellular biocatalysts produced by agaric basidiomycetes such as Agrocybe aegerita or Coprinellus radians catalyze reactions--for example, the peroxygenation of naphthalene, toluene, dibenzothiophene, or pyridine--which are actually attributed to cytochrome P450 monooxygenases. Here, for the first time, genetic information is presented on this new group of peroxide-consuming enzymes. The gene of A. aegerita peroxygenase (apo1) was identified on the level of messenger RNA and genomic DNA. The gene sequence was affirmed by peptide sequences obtained through an Edman degradation and de novo peptide sequencing of the purified enzyme. Quantitative real-time reverse transcriptase polymerase chain reaction demonstrated that the course of enzyme activity correlated well with that of mRNA signals for apo1 in A. aegerita. The full-length sequences of A. aegerita peroxygenase as well as a partial sequence of C. radians peroxygenase confirmed the enzymes' affiliation to the heme-thiolate proteins. The sequences revealed no homology to classic peroxidases, cytochrome P450 enzymes, and only little homology (\u0026lt;30%) to fungal chloroperoxidase produced by the ascomycete Caldariomyces fumago (and this only in the N-terminal part of the protein comprising the heme-binding region and part of the distal heme pocket). This fact reinforces the novelty of APO proteins. On the other hand, homology retrievals in genetic databases resulted in the identification of various APO homologous genes and transcripts, particularly among the agaric fungi, indicating APO's widespread occurrence in the fungal kingdom."}],"geoLocations":[],"fundingReferences":[],"url":"https://boris-portal.unibe.ch/entities/publication/c73f1f0d-7ec2-40c9-bef1-c41b27852457","contentUrl":null,"metadataVersion":4,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2022-03-10T15:43:52Z","registered":"2022-03-10T15:43:54Z","published":null,"updated":"2026-09-08T01:37:11Z"},"relationships":{"client":{"data":{"id":"unibe.boris-portal","type":"clients"}}}},{"id":"10.48620/92778","type":"dois","attributes":{"doi":"10.48620/92778","identifiers":[],"creators":[{"affiliation":["Department of Chemistry, Biochemistry and Pharmaceutical Sciences - Group Professor Paradisi (Pharma"],"name":"Pillet, Lauriane","nameIdentifiers":[]},{"name":"Fernández Reguerio, Cristina Lía","affiliation":[],"nameIdentifiers":[]},{"affiliation":["Department of Chemistry, Biochemistry and Pharmaceutical Sciences"],"name":"Busch, Markus Richard","nameIdentifiers":[]},{"name":"Roura Padrosa, David","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0001-6324-8722"}],"affiliation":[]},{"affiliation":["Department of Chemistry, Biochemistry and Pharmaceutical Sciences - Group Professor Paradisi"],"name":"Paradisi, Francesca","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0003-1704-0642"}]}],"titles":[{"title":"A novel ene-reductase from Halomonas elongata for flow biocatalytic synthesis of 3-phenylpropionaldehyde and sustainable indigo-carmine dyeing."}],"publisher":"University of Bern","container":{},"publicationYear":2025,"subjects":[],"contributors":[],"dates":[{"date":"2025-11-06","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"JournalArticle","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Text"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsUri":"http://purl.org/coar/access_right/c_abf2","rights":"open.access"}],"descriptions":[{"descriptionType":"Abstract","description":"In order to broaden the toolbox of enzymes available for biocatalytic reductions of carbon-carbon double bonds, we investigated four promising ene-reductases (ERs) stemming from extremophilic organisms or showing homology with thermophilic ERs. The novel ene-reductase from the halophilic organism Halomonas elongata showed consistently high activity across a range of tested substrates. Upon immobilisation of the ERs, the flow biocatalytic ene-reduction of cinnamaldhehyde into 3-phenylpropionaldehyde was successfully achieved with an intensification of the process of 62-fold with respect to batch (2173.9 mg L-1 h-1 and 34.7 mg L-1 h-1, respectively). Additionally, to expand the scope of ERs applications, we describe a proof-of concept of a novel enzymatic cascade to convert indole to indigo using an unspecific peroxygenase, and its subsequent reduction to the water-soluble leuco-indigo. In addition, the co-production of the valuable pharmaceuticals precursor 2-oxindole was demonstrated."}],"geoLocations":[],"fundingReferences":[],"url":"https://boris-portal.unibe.ch/handle/20.500.12422/223640","contentUrl":null,"metadataVersion":4,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2025-12-02T12:00:22Z","registered":"2025-12-02T12:00:56Z","published":null,"updated":"2026-09-07T18:52:47Z"},"relationships":{"client":{"data":{"id":"unibe.boris-portal","type":"clients"}}}},{"id":"10.15480/882.8794","type":"dois","attributes":{"doi":"10.15480/882.8794","identifiers":[{"identifier":"New Biotechnology 78: 95-104 (2023-12-25)","identifierType":"citation"},{"identifier":"https://hdl.handle.net/11420/44044","identifierType":"uri"}],"creators":[{"nameType":"Personal","givenName":"Giovanni","familyName":"Sayoga","name":"Sayoga, Giovanni","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0002-7329-9782"},{"nameIdentifierScheme":"GND","schemeUri":"https://d-nb.info/gnd/","nameIdentifier":"1379391172"}],"affiliation":[]},{"nameType":"Personal","givenName":"Victoria","familyName":"Bueschler","name":"Bueschler, Victoria","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0001-8942-1896"},{"nameIdentifierScheme":"GND","schemeUri":"https://d-nb.info/gnd/","nameIdentifier":"1343613531"}],"affiliation":[]},{"nameType":"Personal","givenName":"Hubert","familyName":"Beisch","name":"Beisch, Hubert","affiliation":[],"nameIdentifiers":[]},{"nameType":"Personal","givenName":"Tyll","familyName":"Utesch","name":"Utesch, Tyll","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0001-7514-7013"},{"nameIdentifierScheme":"GND","schemeUri":"https://d-nb.info/gnd/","nameIdentifier":"1200643410"}],"affiliation":[]},{"nameType":"Personal","givenName":"Dirk","familyName":"Holtmann","name":"Holtmann, Dirk","nameIdentifiers":[{"nameIdentifierScheme":"GND","schemeUri":"https://d-nb.info/gnd/","nameIdentifier":"130505641"}],"affiliation":[]},{"nameType":"Personal","givenName":"Bodo","familyName":"Fiedler","name":"Fiedler, Bodo","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0002-2734-1353"},{"nameIdentifierScheme":"GND","schemeUri":"https://d-nb.info/gnd/","nameIdentifier":"120262258"}],"affiliation":[]},{"nameType":"Personal","givenName":"Daniel","familyName":"Ohde","name":"Ohde, Daniel","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0002-5482-3534"},{"nameIdentifierScheme":"GND","schemeUri":"https://d-nb.info/gnd/","nameIdentifier":"1201364108"}],"affiliation":[]},{"nameType":"Personal","givenName":"Andreas","familyName":"Liese","name":"Liese, Andreas","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0002-4867-9935"},{"nameIdentifierScheme":"GND","schemeUri":"https://d-nb.info/gnd/","nameIdentifier":"12031830X"}],"affiliation":[]}],"titles":[{"title":"Electrochemical H₂O₂ - stat mode as reaction concept to improve the process performance of an unspecific peroxygenase"}],"publisher":"Elsevier","container":{"identifier":"1871-6784","firstPage":"95","lastPage":"104","identifierType":"ISSN","type":"Series","title":"New biotechnology"},"publicationYear":2023,"subjects":[{"subject":"Biocatalysis"},{"subject":"Bioelectrocatalysis"},{"subject":"Bioelectrochemical system"},{"subject":"Electrosynthesis"},{"subject":"Hydrogen peroxide"},{"classificationCode":"660","subject":"Chemical Engineering","subjectScheme":"DDC"}],"contributors":[{"name":"TUHH Universitätsbibliothek","contributorType":"DataManager","affiliation":[],"nameIdentifiers":[]},{"name":"TUHH Universitätsbibliothek","contributorType":"HostingInstitution","affiliation":[],"nameIdentifiers":[]}],"dates":[{"date":"2023-11-02","dateType":"Accepted"},{"date":"2023-11-02","dateType":"Available"},{"date":"2023-12-25","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"JournalArticle","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Journal Article"},"relatedIdentifiers":[{"relationType":"IsIdenticalTo","relatedIdentifier":"10.1016/j.nbt.2023.10.007","relatedIdentifierType":"DOI"}],"relatedItems":[{"relationType":"IsPublishedIn","relatedItemIdentifier":{"relatedItemIdentifier":"1871-6784","relatedItemIdentifierType":"ISSN"},"lastPage":"104","firstPage":"95","relatedItemType":"Journal","creators":[],"publisher":"Elsevier","publicationYear":"2023","titles":[{"title":"New biotechnology"}],"contributors":[]}],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","rightsIdentifier":"cc-by-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"The electroenzymatic hydroxylation of 4-ethylbenzoic acid catalyzed by the recombinant unspecific peroxygenase from the fungus Agrocybe aegerita (rAaeUPO) was performed in a gas diffusion electrode (GDE)-based system. Enzyme stability and productivity are significantly affected by the way the co-substrate hydrogen peroxide (H2O2) is supplied. In this study, two in-situ electrogeneration modes of H2O2 were established and compared. Experiments under galvanostatic conditions (constant productivity of H2O2) were conducted at current densities spanning from 0.8 mA cm−2 to 6.4 mA cm−2. For comparison, experiments under H2O2-stat mode (constant H2O2 concentration) were performed. Here, four H2O2 concentrations between 0.06 mM and 0.28 mM were tested. A maximum H2O2 productivity of 5.5 µM min−1 cm−2 and productivity of 10.5 g L−1 d−1 were achieved under the galvanostatic condition at 6.4 mA cm−2. Meanwhile, the highest total turnover number (TTN) of 710,000 mol mol−1 and turnover frequency (TOF) of 87.5 s−1 were obtained under the H2O2-stat mode at concentration limits of 0.15 mM and 0.28 mM, respectively. The most favorable outcome in terms of maximum achievable TTN, TOF and productivity was found under the H2O2-stat mode at concentration limit of 0.2 mM. Here, a TTN of 655,000 mol mol−1, a TOF of 80.3 s−1 and a productivity of 6.1 g L−1 d−1 were achieved. The electrochemical H2O2-stat mode not only offers a promising alternative reaction concept to the well-established galvanostatic mode but also enhances the process performance of unspecific peroxygenases."}],"geoLocations":[],"fundingReferences":[{"funderIdentifierType":"Crossref Funder ID","funderName":"Deutsche Forschungsgemeinschaft (DFG)","funderIdentifier":"https://doi.org/10.13039/501100001659","schemeUri":"https://www.crossref.org/services/funder-registry/","awardTitle":"SPP 2240: Chemoenzymatic reaction cascade in an All-in-One electrochemical system with in situ supply of H2O2 for biosynthesis in aqueous and organic media","awardNumber":"LI 899/13-1; FI 688/16-1"}],"url":"https://tore.tuhh.de/handle/11420/44044","contentUrl":null,"metadataVersion":7,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2023-11-02T12:02:19Z","registered":"2023-11-02T12:02:45Z","published":null,"updated":"2026-09-02T00:50:40Z"},"relationships":{"client":{"data":{"id":"tib.tuhh","type":"clients"}}}},{"id":"10.5281/zenodo.16928069","type":"dois","attributes":{"doi":"10.5281/zenodo.16928069","identifiers":[],"creators":[{"nameType":"Personal","affiliation":["Barcelona Supercomputing Center","Universitat Internacional de Catalunya"],"givenName":"Martin","familyName":"Floor","name":"Floor, Martin","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0001-8453-0815"}]},{"nameType":"Personal","affiliation":["ICREA -Institucio Catalana de Recerca  i Estudis Avançats","Barcelona Supercomputing Center"],"givenName":"Victor","familyName":"Guallar","name":"Guallar, Victor","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0002-4580-1114"}]}],"titles":[{"title":"Unspecific peroxygenase enzyme sequences curated by PSI-BLAST, InterProScan fold filtering, and catalytic motif conservation"}],"publisher":"Zenodo","container":{},"publicationYear":2025,"subjects":[{"subject":"Unspecific peroxygenase"}],"contributors":[],"dates":[{"date":"2025-08-25","dateType":"Issued"},{"date":"2024-03-22","dateType":"Collected"}],"language":null,"types":{"schemaOrg":"Dataset","resourceTypeGeneral":"Dataset","citeproc":"dataset","bibtex":"misc","ris":"DATA","resourceType":""},"relatedIdentifiers":[{"relationType":"HasVersion","relatedIdentifier":"10.5281/zenodo.16928070","relatedIdentifierType":"DOI"}],"relatedItems":[],"sizes":[],"formats":[],"version":"001","rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","rightsIdentifier":"cc-by-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"Unspecific peroxygenase (UPO) sequences compiled through a multi-stage process:Literature-derived sequences from Hofrichter et al. (2022) were combined with additional UPO sequences obtained in OxyLipids national project (TED2021-129264B-C31/MICIU/AEI/10.13039/501100011033/European Union NextGenerationEU/PRTR) through hidden Markov model (HMM) searches.This combined seed set was used to perform PSI-BLAST searches against UniProtKB/TrEMBL, run for multiple iterations to expand the sequence set.All resulting sequences were annotated with InterProScan, and only those assigned to the Chloroperoxidase-like superfamily fold were retained.Sequences were further filtered to ensure the presence of the PCP motif around the coordinating cysteine and a conserved catalytic salt bridge typical of UPOs."}],"geoLocations":[],"fundingReferences":[{"funderIdentifierType":"Crossref Funder ID","funderName":"European Commission","funderIdentifier":"10.13039/501100000780","awardTitle":"Robust industrial biocatalysts with peroxygenase, phenol-oxidase or furfuryl-oxidase activities from bacterial and fungal hosts","awardNumber":"101135119"}],"url":"https://zenodo.org/doi/10.5281/zenodo.16928069","contentUrl":null,"metadataVersion":2,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"api","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":2,"versionOfCount":1,"created":"2025-08-25T11:51:07Z","registered":"2025-08-25T11:51:07Z","published":null,"updated":"2026-08-28T01:42:05Z"},"relationships":{"client":{"data":{"id":"cern.zenodo","type":"clients"}}}},{"id":"10.5281/zenodo.16928070","type":"dois","attributes":{"doi":"10.5281/zenodo.16928070","identifiers":[{"identifier":"oai:zenodo.org:16928070","identifierType":"oai"}],"creators":[{"nameType":"Personal","affiliation":["Barcelona Supercomputing Center","Universitat Internacional de Catalunya"],"givenName":"Martin","familyName":"Floor","name":"Floor, Martin","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0001-8453-0815"}]},{"nameType":"Personal","affiliation":["ICREA -Institucio Catalana de Recerca  i Estudis Avançats","Barcelona Supercomputing Center"],"givenName":"Victor","familyName":"Guallar","name":"Guallar, Victor","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0002-4580-1114"}]}],"titles":[{"title":"Unspecific peroxygenase enzyme sequences curated by PSI-BLAST, InterProScan fold filtering, and catalytic motif conservation"}],"publisher":"Zenodo","container":{},"publicationYear":2025,"subjects":[{"subject":"Unspecific peroxygenase"}],"contributors":[],"dates":[{"date":"2025-08-25","dateType":"Issued"},{"date":"2024-03-22","dateType":"Collected"}],"language":null,"types":{"schemaOrg":"Dataset","resourceTypeGeneral":"Dataset","citeproc":"dataset","bibtex":"misc","ris":"DATA","resourceType":""},"relatedIdentifiers":[{"relationType":"IsVersionOf","relatedIdentifier":"10.5281/zenodo.16928069","relatedIdentifierType":"DOI"}],"relatedItems":[],"sizes":[],"formats":[],"version":"001","rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","rightsIdentifier":"cc-by-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"Unspecific peroxygenase (UPO) sequences compiled through a multi-stage process:Literature-derived sequences from Hofrichter et al. (2022) were combined with additional UPO sequences obtained in OxyLipids national project (TED2021-129264B-C31/MICIU/AEI/10.13039/501100011033/European Union NextGenerationEU/PRTR) through hidden Markov model (HMM) searches.This combined seed set was used to perform PSI-BLAST searches against UniProtKB/TrEMBL, run for multiple iterations to expand the sequence set.All resulting sequences were annotated with InterProScan, and only those assigned to the Chloroperoxidase-like superfamily fold were retained.Sequences were further filtered to ensure the presence of the PCP motif around the coordinating cysteine and a conserved catalytic salt bridge typical of UPOs."}],"geoLocations":[],"fundingReferences":[{"funderIdentifierType":"Crossref Funder ID","funderName":"European Commission","funderIdentifier":"10.13039/501100000780","awardTitle":"Robust industrial biocatalysts with peroxygenase, phenol-oxidase or furfuryl-oxidase activities from bacterial and fungal hosts","awardNumber":"101135119"}],"url":"https://zenodo.org/doi/10.5281/zenodo.16928070","contentUrl":null,"metadataVersion":0,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"api","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":1,"created":"2025-08-25T11:51:07Z","registered":"2025-08-25T11:51:07Z","published":null,"updated":"2026-08-28T01:42:04Z"},"relationships":{"client":{"data":{"id":"cern.zenodo","type":"clients"}}}},{"id":"10.15480/882.18006","type":"dois","attributes":{"doi":"10.15480/882.18006","identifiers":[{"identifier":"Technische Universität Hamburg (2025)","identifierType":"citation"},{"identifier":"https://hdl.handle.net/11420/64439","identifierType":"uri"}],"creators":[{"nameType":"Personal","givenName":"Andreas","familyName":"Liese","name":"Liese, Andreas","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0002-4867-9935"},{"nameIdentifierScheme":"GND","schemeUri":"https://d-nb.info/gnd/","nameIdentifier":"12031830X"}],"affiliation":[]},{"nameType":"Personal","givenName":"Dirk","familyName":"Holtmann","name":"Holtmann, Dirk","nameIdentifiers":[{"nameIdentifierScheme":"GND","schemeUri":"https://d-nb.info/gnd/","nameIdentifier":"130505641"}],"affiliation":[]}],"titles":[{"title":"Enzyme and reaction engineering of unspecific peroxygenase driven hydroxylation of butane (BUPOx)"}],"publisher":"TUHH Universitätsbibliothek","container":{},"publicationYear":2025,"subjects":[{"subject":"enzyme catalysis"},{"subject":"unspecific peroxygenase (UPO)"},{"subject":"biotechnology"},{"subject":"bubble column"},{"classificationCode":"6","subject":"Technology::660: Chemistry; Chemical Engineering::660.6: Biotechnology","subjectScheme":"DDC"}],"contributors":[{"name":"TUHH Universitätsbibliothek","contributorType":"DataManager","affiliation":[],"nameIdentifiers":[]},{"name":"TUHH Universitätsbibliothek","contributorType":"HostingInstitution","affiliation":[],"nameIdentifiers":[]}],"dates":[{"date":"2026-08-24","dateType":"Accepted"},{"date":"2026-08-24","dateType":"Available"},{"date":"2025-03-31","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"Report","resourceTypeGeneral":"Report","citeproc":"report","bibtex":"techreport","ris":"RPRT","resourceType":"Report"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","rightsIdentifier":"cc-by-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"In this study, scalable biocatalytic processes were developed in which unspecific peroxygenase (UPO) is used for selective oxyfunctionalization. The most important challenges in terms of enzyme production and stability, controlled electrochemical generation of cosubstrates, in situ product removal and semi-continuous operability were addressed. Robust UPO expression and downstream strategies enabled continuous operation, while detailed kinetic characterisation showed that a precise balance between substrate and hydrogen peroxide concentrations is required to prevent oxidative inactivation. Immobilised UPO such as His-tag, Twin-Strep-labelled and YSD (yeast surface display) variants, achieved high activity retention and operational stability in fluidised bed systems, enabling longer reaction cycles and simplified product recovery."}],"geoLocations":[],"fundingReferences":[{"funderIdentifierType":"Crossref Funder ID","funderName":"Deutsche Forschungsgemeinschaft (DFG)","funderIdentifier":"https://doi.org/10.13039/501100001659","schemeUri":"https://www.crossref.org/services/funder-registry/","awardTitle":"Enzym- und Reaktionstechnik der unspezifischen Peroxygenase katalysierten Hydroxylierung von Butan (BUPOx)","awardNumber":"LI 899/18-1"}],"url":"https://tore.tuhh.de/handle/11420/64439","contentUrl":null,"metadataVersion":0,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2026-08-24T04:53:15Z","registered":"2026-08-24T04:53:48Z","published":null,"updated":"2026-08-24T04:54:25Z"},"relationships":{"client":{"data":{"id":"tib.tuhh","type":"clients"}}}},{"id":"10.34657/5826","type":"dois","attributes":{"doi":"10.34657/5826","identifiers":[],"creators":[{"name":"Ingenbosch, Kim N.","affiliation":[],"nameIdentifiers":[]},{"name":"Quint, Stephan","affiliation":[],"nameIdentifiers":[]},{"name":"Dyllick-Brenzinger, Melanie","affiliation":[],"nameIdentifiers":[]},{"name":"Wunschik, Dennis S.","affiliation":[],"nameIdentifiers":[]},{"name":"Kiebist, Jan","affiliation":[],"nameIdentifiers":[]},{"name":"Süss, Philipp","affiliation":[],"nameIdentifiers":[]},{"name":"Liebelt, Ute","affiliation":[],"nameIdentifiers":[]},{"name":"Zuhse, Ralf","affiliation":[],"nameIdentifiers":[]},{"name":"Menyes, Ulf","affiliation":[],"nameIdentifiers":[]},{"name":"Scheibner, Katrin","affiliation":[],"nameIdentifiers":[]},{"name":"Mayer, Christian","affiliation":[],"nameIdentifiers":[]},{"name":"Opwis, Klaus","affiliation":[],"nameIdentifiers":[]},{"name":"Gutmann, Jochen S.","affiliation":[],"nameIdentifiers":[]},{"name":"Hoffmann-Jacobsen, Kerstin","affiliation":[],"nameIdentifiers":[]}],"titles":[{"lang":"eng","title":"Singlet-Oxygen Generation by Peroxidases and Peroxygenases for Chemoenzymatic Synthesis"}],"publisher":"Weinheim : Wiley-VCH","container":{},"publicationYear":2020,"subjects":[{"subject":"540","lang":"eng","subjectScheme":"ddc"},{"subject":"chemo-enzymatic synthesis","lang":"eng","subjectScheme":"other"},{"subject":"fluorescence","lang":"eng","subjectScheme":"other"},{"subject":"peroxidase","lang":"eng","subjectScheme":"other"},{"subject":"peroxygenase","lang":"eng","subjectScheme":"other"},{"subject":"singlet oxygen","lang":"eng","subjectScheme":"other"},{"subject":"singlet oxygen sensor green","lang":"eng","subjectScheme":"other"}],"contributors":[{"name":"Technische Informationsbibliothek (TIB)","contributorType":"DataManager","affiliation":[],"nameIdentifiers":[]},{"name":"Technische Informationsbibliothek (TIB)","contributorType":"HostingInstitution","affiliation":[],"nameIdentifiers":[]}],"dates":[{"date":"2021-09-10","dateType":"Accepted"},{"date":"2021-09-10","dateType":"Available"},{"date":"2020","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"JournalArticle","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Article"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rights":"CC BY 4.0 International"},{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","rightsIdentifier":"cc-by-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"Singlet oxygen is a reactive oxygen species undesired in living cells but a rare and valuable reagent in chemical synthesis. We present a fluorescence spectroscopic analysis of the singlet-oxygen formation activity of commercial peroxidases and novel peroxygenases. Singlet-oxygen sensor green (SOSG) is used as fluorogenic singlet oxygen trap. Establishing a kinetic model for the reaction cascade to the fluorescent SOSG endoperoxide permits a kinetic analysis of enzymatic singlet-oxygen formation. All peroxidases and peroxygenases show singlet-oxygen formation. No singlet oxygen activity could be found for any catalase under investigation. Substrate inhibition is observed for all reactive enzymes. The commercial dye-decolorizing peroxidase industrially used for dairy bleaching shows the highest singlet-oxygen activity and the lowest inhibition. This enzyme was immobilized on a textile carrier and successfully applied for a chemical synthesis. Here, ascaridole was synthesized via enzymatically produced singlet oxygen. © 2020 Wiley-VCH GmbH","lang":"eng"}],"geoLocations":[],"fundingReferences":[],"url":"https://oa.tib.eu/renate/handle/123456789/6779","contentUrl":null,"metadataVersion":10,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2021-09-10T06:45:26Z","registered":"2021-09-10T07:00:08Z","published":null,"updated":"2026-08-20T11:17:56Z"},"relationships":{"client":{"data":{"id":"tib.tibrepo","type":"clients"}}}},{"id":"10.34657/17846","type":"dois","attributes":{"doi":"10.34657/17846","identifiers":[],"creators":[{"name":"De Santis, Piera","affiliation":[],"nameIdentifiers":[]},{"name":"Wegstein, Deborah","affiliation":[],"nameIdentifiers":[]},{"name":"Burek, Bastien O.","affiliation":[],"nameIdentifiers":[]},{"name":"Patzsch, Jacqueline","affiliation":[],"nameIdentifiers":[]},{"name":"Alcalde, Miguel","affiliation":[],"nameIdentifiers":[]},{"name":"Kroutil, Wolfgang","affiliation":[],"nameIdentifiers":[]},{"name":"Bloh, Jonathan Z.","affiliation":[],"nameIdentifiers":[]},{"name":"Kara, Selin","affiliation":[],"nameIdentifiers":[]}],"titles":[{"lang":"eng","title":"Robust Light Driven Enzymatic Oxyfunctionalization via Immobilization of Unspecific Peroxygenase"}],"publisher":"Weinheim : Wiley-VCH","container":{},"publicationYear":2023,"subjects":[{"subject":"540","lang":"","subjectScheme":"ddc"},{"subject":"photocatalysis","lang":"eng","subjectScheme":"other"},{"subject":"biocatalysis","lang":"eng","subjectScheme":"other"},{"subject":"peroxygenases","lang":"eng","subjectScheme":"other"},{"subject":"g-C3N4","lang":"eng","subjectScheme":"other"},{"subject":"immobilized enzyme","lang":"eng","subjectScheme":"other"}],"contributors":[{"name":"Technische Informationsbibliothek (TIB)","contributorType":"DataManager","affiliation":[],"nameIdentifiers":[]},{"name":"Technische Informationsbibliothek (TIB)","contributorType":"HostingInstitution","affiliation":[],"nameIdentifiers":[]}],"dates":[{"date":"2025-03-27","dateType":"Accepted"},{"date":"2025-03-27","dateType":"Available"},{"date":"2023-06-25","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"JournalArticle","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Article"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rights":"CC BY-NC 4.0 International"},{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution Non Commercial 4.0 International","rightsIdentifier":"cc-by-nc-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"Unspecific peroxygenases have attracted interest in synthetic chemistry, especially for the oxidative activation of C−H bonds, as they only require hydrogen peroxide (H2O2) instead of a cofactor. Due to their instability in even small amounts of H2O2, different strategies like enzyme immobilization or in situ H2O2 production have been developed to improve the stability of these enzymes. While most strategies have been studied separately, a combination of photocatalysis with immobilized enzymes was only recently reported. To show the advantages and limiting factors of immobilized enzyme in a photobiocatalytic reaction, a comparison is made between free and immobilized enzymes. Adjustment of critical parameters such as (i) enzyme and substrate concentration, (ii) illumination wavelength and (iii) light intensity results in significantly increased enzyme stabilities of the immobilized variant. Moreover, under optimized conditions a turnover number of 334,500 was reached.","lang":"eng"}],"geoLocations":[],"fundingReferences":[],"url":"https://oa.tib.eu/renate/handle/123456789/18827","contentUrl":null,"metadataVersion":2,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2025-03-27T10:45:27Z","registered":"2025-03-27T10:45:28Z","published":null,"updated":"2026-08-20T11:02:39Z"},"relationships":{"client":{"data":{"id":"tib.tibrepo","type":"clients"}}}},{"id":"10.5281/zenodo.19047656","type":"dois","attributes":{"doi":"10.5281/zenodo.19047656","identifiers":[],"creators":[{"nameType":"Personal","affiliation":["Universitat Jaume I"],"givenName":"Katarzyna","familyName":"Świderek","name":"Świderek, Katarzyna","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0002-7528-1551"}]},{"nameType":"Personal","affiliation":["Universitat Jaume I"],"givenName":"Vicent","familyName":"Moliner","name":"Moliner, Vicent","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0002-3665-3391"}]}],"titles":[{"title":"Directed evolution of a promiscuous fungal peroxygenase from Chaetomium globosum"}],"publisher":"Zenodo","container":{},"publicationYear":2026,"subjects":[],"contributors":[{"nameType":"Personal","affiliation":["Institute of Catalysis and Petrochemistry, ICP, CSIC"],"givenName":"Miguel","familyName":"Alcalde","name":"Alcalde, Miguel","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0001-6780-7616"}],"contributorType":"ProjectLeader"},{"nameType":"Personal","givenName":"David","familyName":"Upp","name":"Upp, David","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0002-6715-5862"}],"contributorType":"ProjectMember","affiliation":[]}],"dates":[{"date":"2026-03-16","dateType":"Issued"}],"language":null,"types":{"schemaOrg":"Dataset","resourceTypeGeneral":"Dataset","citeproc":"dataset","bibtex":"misc","ris":"DATA","resourceType":""},"relatedIdentifiers":[{"relationType":"HasVersion","relatedIdentifier":"10.5281/zenodo.19047657","relatedIdentifierType":"DOI"}],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","rightsIdentifier":"cc-by-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"Long unbiased molecular dynamics (MD) simulations were conducted on the parental CglUPO and the AckBar variant to shed light on the observed opposite enantioselectivities in the oxidation of 1,2,3,4, tetrahydronaphthalene, (THN), as well as to reveal the origin of the observed anti-Markovnikov oxidation of styrene (STR). Reduced molecular dynamics (MD) trajectories (2,500 snapshots each, representing 0.5 μs of simulation in each replica) for both THN oxidation catalyzed by CglUPO and the AckBar and the epoxidation versus anti-Markovnikov Wacker oxidation selectivity in the reaction with styrene are provided."}],"geoLocations":[],"fundingReferences":[],"url":"https://zenodo.org/doi/10.5281/zenodo.19047656","contentUrl":null,"metadataVersion":1,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"api","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":2,"versionOfCount":1,"created":"2026-04-13T08:11:15Z","registered":"2026-04-13T08:11:16Z","published":null,"updated":"2026-08-15T17:30:40Z"},"relationships":{"client":{"data":{"id":"cern.zenodo","type":"clients"}}}},{"id":"10.5281/zenodo.19047657","type":"dois","attributes":{"doi":"10.5281/zenodo.19047657","identifiers":[{"identifier":"oai:zenodo.org:19047657","identifierType":"oai"}],"creators":[{"nameType":"Personal","affiliation":["Universitat Jaume I"],"givenName":"Katarzyna","familyName":"Świderek","name":"Świderek, Katarzyna","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0002-7528-1551"}]},{"nameType":"Personal","affiliation":["Universitat Jaume I"],"givenName":"Vicent","familyName":"Moliner","name":"Moliner, Vicent","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0002-3665-3391"}]}],"titles":[{"title":"Directed evolution of a promiscuous fungal peroxygenase from Chaetomium globosum"}],"publisher":"Zenodo","container":{},"publicationYear":2026,"subjects":[],"contributors":[{"nameType":"Personal","affiliation":["Institute of Catalysis and Petrochemistry, ICP, CSIC"],"givenName":"Miguel","familyName":"Alcalde","name":"Alcalde, Miguel","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0001-6780-7616"}],"contributorType":"ProjectLeader"},{"nameType":"Personal","givenName":"David","familyName":"Upp","name":"Upp, David","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","nameIdentifier":"0000-0002-6715-5862"}],"contributorType":"ProjectMember","affiliation":[]}],"dates":[{"date":"2026-03-16","dateType":"Issued"}],"language":null,"types":{"schemaOrg":"Dataset","resourceTypeGeneral":"Dataset","citeproc":"dataset","bibtex":"misc","ris":"DATA","resourceType":""},"relatedIdentifiers":[{"relationType":"IsVersionOf","relatedIdentifier":"10.5281/zenodo.19047656","relatedIdentifierType":"DOI"}],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","rightsIdentifier":"cc-by-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"Long unbiased molecular dynamics (MD) simulations were conducted on the parental CglUPO and the AckBar variant to shed light on the observed opposite enantioselectivities in the oxidation of 1,2,3,4, tetrahydronaphthalene, (THN), as well as to reveal the origin of the observed anti-Markovnikov oxidation of styrene (STR). Reduced molecular dynamics (MD) trajectories (2,500 snapshots each, representing 0.5 μs of simulation in each replica) for both THN oxidation catalyzed by CglUPO and the AckBar and the epoxidation versus anti-Markovnikov Wacker oxidation selectivity in the reaction with styrene are provided."}],"geoLocations":[],"fundingReferences":[],"url":"https://zenodo.org/doi/10.5281/zenodo.19047657","contentUrl":null,"metadataVersion":0,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"api","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":1,"created":"2026-04-13T08:11:16Z","registered":"2026-04-13T08:11:16Z","published":null,"updated":"2026-08-15T17:30:39Z"},"relationships":{"client":{"data":{"id":"cern.zenodo","type":"clients"}}}},{"id":"10.82308/10876","type":"dois","attributes":{"doi":"10.82308/10876","identifiers":[{"identifier":"hyrax:b5644z26g","identifierType":"other"},{"identifier":"https://hdl.handle.net/20.500.14905/100720","identifierType":"uri"},{"identifier":"1428737197","identifierType":"oclc"}],"creators":[{"name":"Heikham, Russiachand Singh","affiliation":[],"nameIdentifiers":[]}],"titles":[{"title":"Identification of candidate R genes in wheat, Sumai-3 and Pasteur against Fusarium head blight based on transcriptomics, metabolomics, and single nucleotide polymorphism"}],"publisher":"McGill University","container":{},"publicationYear":2023,"subjects":[{"subject":"Plant Science","lang":""}],"contributors":[{"name":"McGill University","contributorType":"DataManager","affiliation":[],"nameIdentifiers":[]},{"name":"McGill University","contributorType":"HostingInstitution","affiliation":[],"nameIdentifiers":[]},{"name":"Kushalappa, Ajjamada (Supervisor)","contributorType":"Supervisor","affiliation":[],"nameIdentifiers":[]}],"dates":[{"date":"2026-03-18","dateType":"Accepted"},{"date":"2023","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"Thesis","resourceTypeGeneral":"Dissertation","citeproc":"thesis","bibtex":"phdthesis","ris":"THES","resourceType":"https://vocabularies.coar-repositories.org/resource_types/c_46ec/"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rights":"All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated."}],"descriptions":[{"descriptionType":"Other","description":"Kushalappa, Ajjamada (Supervisor)","lang":""},{"descriptionType":"Abstract","description":"La fusariose de l'épi (FHB) causée par Fusarium graminearum (Fg) est l'une des maladies destructrices du blé qui provoque de graves épidémies et des pertes de rendement. De plus, il détériore la qualité des grains en accumulant des mycotoxines, nocives pour la santé humaine et animale. La résistance à la fusariose chez le blé est quantitative, et plus de 100 locus de caractères quantitatifs (QTL) ont été cartographiés génétiquement chez le blé, conférant des effets de résistance majeurs et mineurs. Sumai-3 et ses dérivés présentent un niveau élevé de résistance à la FHB et ont été utilisés dans des programmes de sélection de résistance à la FHB dans le monde entier.Plusieurs études omiques ont été utilisées pour identifier les gènes de résistance à la FHB et expliquer leurs mécanismes de résistance. Suite à l'invasion de pathogènes, plusieurs métabolites de résistance sont produits dans différentes voies contrôlées par les gènes R biosynthétiques et régulateurs. Ces gènes sont localisés dans différents QTL ou chromosomes. Des mutations dans ces gènes R conduisent à la susceptibilité. Cette étude utilise des génotypes de blé résistants à la FHB (Sumai-3) et sensibles à la FHB (Pasteur) dans des études de transcriptomique et de métabolomique, après Fg et une inoculation fictive. Les échantillons prélevés à 48 hpi et 72 hpi ont été utilisés respectivement dans des études de profilage RNA-Seq et métabolique. Plusieurs algorithmes, k-mer, de novo et des approches d'assemblage basées sur des références ont été utilisés dans des études de transcriptomique et ont révélé plusieurs gènes R dans Sumai-3 et des gènes sensibles ou mutés chez Pasteur. De plus, les cibles de miARN ont été prédites au niveau du transcrit à l'aide de transcrits générés non redondants. Les données RNA-Seq ont également été utilisées pour détecter les mutations (SNPs/InDels) dans la région codante. Un profilage métabolique non ciblé a été utilisé pour identifier la forte abondance de métabolites résistants.La première étude sur l'assemblage de novo et de référence des données de transcriptomes a révélé un certain nombre de gènes dans la lignée Sumai-3 résistante à la FHB de blé (c. -CoA O-méthyltransférase, peroxydase (POD), laccase, agmatine coumaroyltransférase-2 (ACT2), chalcone synthase, trans-cinnamate 4-monooxygénase, anthocyanidine synthase, anthocyanidine réductase, dihydroflavonol-4-réductase et peroxygénase) sont régulés à la hausse qui codent pour des enzymes impliquées dans la biosynthèse de la lignine. Le dépôt de lignine dans la paroi cellulaire conduit à la résistance des plantes aux agents pathogènes. De plus, nous avons trouvé les gènes R laccase (tae-miR6197-5p) et dihydroflavonol-4-réductase (tae-miR9672a-3p) ciblés par les miARN. Dans la deuxième étude, nous avons exploré les SNP/InDels dans les données RNA-Seq et identifié cinq gènes R codants délétères et non synonymes dans le cultivar de blé Pasteur sensible à la FHB (TaPOD, TaACT2, TaDFR, lipoxygénase et protéine de type thaumatine). Les métabolites RR tels que le 4-coumarate, le kaempférol, l'acide hydroxynervonique et le 22-oxodocosanoate se sont avérés moins abondants chez Pasteur. Les gènes R mutés identifiés dans différentes voies métaboliques et leur R régulateur ici peuvent être davantage confirmés dans le cultivar Pasteur sensible au FHB et utilisés dans l'édition du génome pour améliorer la résistance au FHB","lang":"fr"},{"descriptionType":"Abstract","description":"Fusarium head blight (FHB) caused by Fusarium graminearum (Fg) is one of the destructive diseases of wheat that causes severe epidemics and yield losses. In addition, it deteriorates the quality of grains by accumulating mycotoxins, which are harmful to human and animal health. Resistance to FHB in wheat is quantitative, and more than 100 quantitative trait loci (QTL) have been genetically mapped in wheat, conferring major and minor resistance effects. Sumai-3 and its derivatives exhibit a high level of FHB resistance and have been used in FHB resistance breeding programs worldwide.Several OMICs studies have been used to identify the FHB resistance genes and to explain their resistance mechanisms. Following pathogen invasion, several resistance metabolites are produced in different pathways controlled by the biosynthetic and regulatory R genes. These genes are localized in different QTLs or chromosomes. Mutations in these R genes lead to susceptibility. This study employs FHB-resistant (Sumai-3) and FHB-susceptible (Pasteur) wheat genotypes in transcriptomics and metabolomics studies, following Fg and mock inoculation. The samples collected at 48hpi and 72hpi have been used in RNA-Seq and metabolic profiling studies, respectively. Multiple algorithms, k-mer, de novo, and reference-based assembly approaches have been used in transcriptomics studies and revealed several R genes in Sumai-3 and susceptible or mutated genes in Pasteur. Furthermore, miRNA targets have been predicted at the transcript level using non-redundant generated transcripts. RNA-Seq data have also been used to detect the mutations (SNPs /InDels) in the coding region. Untargeted metabolic profiling has been used to identify the high abundance of resistance metabolites.The first study on de novo and reference assembly of transcriptomes data revealed a number of genes in the wheat FHB-resistant line Sumai-3 (i.e., phenylalanine ammonia-lyase, cinnamoyl CoA reductase, hydroxycinnamoyltransferase, caffeic acid 3-O-methyltransferase, caffeoyl-CoA O-methyltransferase, peroxidase (POD), laccase, agmatine coumaroyltransferase-2 (ACT2), chalcone synthase, trans-cinnamate 4-monooxygenase, anthocyanidin synthase, anthocyanidin reductase, dihydroflavonol-4-reductase, and peroxygenase) are up-regulated that encode enzymes involved in lignin biosynthesis. Lignin deposition in the cell wall leads to plant resistance to pathogens. Further, we found R genes laccase (tae-miR6197-5p) and dihydroflavonol-4-reductase (tae-miR9672a-3p) targeted by miRNAs. In the second study, we explored SNPs/InDels in the RNA-Seq data and identified five deleterious and non-synonymous coding R genes in FHB-susceptible wheat cultivar Pasteur (TaPOD, TaACT2, TaDFR, lipoxygenase, and thaumatin-like protein). The RR metabolites such as 4-coumarate, kaempferol, hydroxynervonic acid, and 22-oxodocosanoate were found to have lower abundance in Pasteur. The mutated R genes identified in different metabolic pathways and their regulatory R here can be further confirmed in the FHB-susceptible cultivar Pasteur and used in genome editing to enhance resistance to FHB","lang":"en"}],"geoLocations":[],"fundingReferences":[],"url":"https://mcgill.scholaris.ca/handle/20.500.14905/100720","contentUrl":null,"metadataVersion":1,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2026-05-20T19:52:02Z","registered":"2026-05-20T19:52:03Z","published":null,"updated":"2026-07-30T17:48:39Z"},"relationships":{"client":{"data":{"id":"iyfw.kddaax","type":"clients"}}}},{"id":"10.5445/ir/1000194600","type":"dois","attributes":{"doi":"10.5445/ir/1000194600","identifiers":[],"creators":[{"nameType":"Personal","affiliation":[],"givenName":"Michael","familyName":"Abt","name":"Abt, Michael","nameIdentifiers":[]},{"nameType":"Personal","affiliation":[],"givenName":"Carolin","familyName":"Kienzle","name":"Kienzle, Carolin","nameIdentifiers":[]},{"nameType":"Personal","affiliation":[],"givenName":"Melissa","familyName":"Ditzel","name":"Ditzel, Melissa","nameIdentifiers":[]},{"nameType":"Personal","affiliation":[],"givenName":"Mirco","familyName":"Jestädt","name":"Jestädt, Mirco","nameIdentifiers":[]},{"nameType":"Personal","affiliation":[],"givenName":"Katharina","familyName":"Bleher","name":"Bleher, Katharina","nameIdentifiers":[]},{"nameType":"Personal","affiliation":[],"givenName":"Matthias","familyName":"Franzreb","name":"Franzreb, Matthias","nameIdentifiers":[]},{"nameType":"Personal","affiliation":[],"givenName":"André","familyName":"Tschöpe","name":"Tschöpe, André","nameIdentifiers":[]}],"titles":[{"title":"Application of a three-phase fluidized bed electrode for an electro-enzymatic batch process with the peroxygenase AaeUPO"}],"publisher":"Elsevier","container":{},"publicationYear":2026,"subjects":[{"subject":"Electro-enzymatic"},{"subject":"Fluidized bed electrode"},{"subject":"Unspecific peroxygenase (AaeUPO)"},{"subject":"In-situ H2O2"},{"subject":"Hydroxylation"}],"contributors":[],"dates":[{"date":"2026","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"Text","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Journal Article"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsUri":"info:eu-repo/semantics/openAccess","rights":"Open Access"},{"rightsUri":"https://creativecommons.org/licenses/by/4.0/deed.de","rights":"Creative Commons Namensnennung 4.0 International"}],"descriptions":[{"descriptionType":"Abstract","description":"Electrification of biological syntheses offers a sustainable route to decarbonize chemical production. This requires innovative reactor concepts that combine efficient electrochemical reaction steps with selective biocatalysts. Unspecific peroxygenases (UPOs) are attractive because they hydroxylate non-activated Csingle bondH bonds and need only hydrogen peroxide (H₂O₂) as co-substrate. However, excess H₂O₂ rapidly deactivates UPOs. Electrochemical reactors must therefore generate H₂O₂ in-situ at low, uniform levels while maintaining strong mixing and mass transfer — a capability conventional electrochemical cells struggle to provide. Here, we present the first three-phase electrochemical fluidized bed reactor (gas–liquid–solid) for combined electro-enzymatic synthesis. This reactor utilizes conductive graphite particles as a fluidized electrode on which oxygen reduction generates H₂O₂ throughout the particle bed, while air sparging resupplies O₂ and drives mixing, enhancing mass transfer. Using the unspecific peroxygenase from Agrocybe aegerita (AaeUPO) as a model enzyme, we successfully optimized the electrochemical H₂O₂ generation rate to maintain non-inhibitory H2O2 concentrations below 0.2 mM and achieved a high current efficiency of 54.5 ± 12.5% for enzymatic product formation. Moreover, the batch process demonstrated scalability, as increasing the enzyme concentration enabled a Y$_{HEBA/EBA}$ of ~100% at even higher H₂O₂ generation rates, resulting in a space-time yield (STY) of 38.83 ± 0.32 g/(L·d) for the hydroxylation of 4-ethylbenzoic acid (EBA) to 4-(1-hydroxyethyl)benzoic acid (HEBA). These results establish the electrochemical fluidized bed reactor as a highly efficient platform for electro-enzymatic synthesis, particularly for processes requiring in-situ co-substrate generation."}],"geoLocations":[],"fundingReferences":[],"url":"https://publikationen.bibliothek.kit.edu/1000194600","contentUrl":null,"metadataVersion":0,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2026-06-25T11:06:06Z","registered":"2026-06-25T11:06:06Z","published":null,"updated":"2026-06-25T11:06:06Z"},"relationships":{"client":{"data":{"id":"tib.kit","type":"clients"}}}},{"id":"10.48550/arxiv.2606.21370","type":"dois","attributes":{"doi":"10.48550/arxiv.2606.21370","identifiers":[{"identifier":"2606.21370","identifierType":"arXiv"}],"creators":[{"nameType":"Personal","givenName":"Hanna-Friederike","familyName":"Poggemann","name":"Poggemann, Hanna-Friederike","affiliation":[],"nameIdentifiers":[]},{"nameType":"Personal","givenName":"Tim","familyName":"Dirks","name":"Dirks, Tim","affiliation":[],"nameIdentifiers":[]},{"nameType":"Personal","givenName":"Timo","familyName":"Jacob","name":"Jacob, Timo","affiliation":[],"nameIdentifiers":[]},{"nameType":"Personal","givenName":"Christoph","familyName":"Jung","name":"Jung, Christoph","affiliation":[],"nameIdentifiers":[]}],"titles":[{"title":"Computationally guided modifications of CviUPO to improve catalytic activity"}],"publisher":"arXiv","container":{},"publicationYear":2026,"subjects":[{"subject":"Biological Physics (physics.bio-ph)","lang":"en","subjectScheme":"arXiv"},{"subject":"FOS: Physical sciences","subjectScheme":"Fields of Science and Technology (FOS)"},{"schemeUri":"http://www.oecd.org/science/inno/38235147.pdf","subject":"FOS: Physical sciences","subjectScheme":"Fields of Science and Technology (FOS)"}],"contributors":[],"dates":[{"date":"2026-06-19T12:21:15Z","dateType":"Submitted","dateInformation":"v1"},{"date":"2026-06-23T00:47:26Z","dateType":"Updated","dateInformation":"v1"},{"date":"2026-06","dateType":"Available","dateInformation":"v1"},{"date":"2026","dateType":"Issued"}],"language":null,"types":{"schemaOrg":"CreativeWork","resourceTypeGeneral":"Preprint","citeproc":"article","bibtex":"misc","ris":"GEN","resourceType":"Article"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":"1","rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","rightsIdentifier":"cc-by-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"Unspecific peroxygenases (UPOs) are promising biocatalysts that selectively oxyfunctionalize saturated hydrocarbons using only hydrogen peroxide as a co-substrate. Peroxide-induced enzyme inactivation makes targeted enzyme engineering essential to mitigate this effect and also enhance catalytic performance. To meet this need, systematic approaches are used, including extensive database studies for rational enzyme design, as well as computational enzyme engineering. In this study, we followed the latter strategy and explored the possibility for computationally-guided modification of UPOs. Specifically, our focus was on uncovering the influence of active site amino acids on the catalytic activity of the enzyme CviUPO. Two mutations were introduced close to the active center, and the changes in the energy barriers leading to the activated complex were investigated in detail by Quantum Mechanics/Molecular Mechanics Nudged Elastic Band simulations. Our studies revealed that a change of the glutamic acid, assisting the catalytic cycle, by the shorter aspartic acid, leads to an increased reaction barrier, probably decreasing the catalytic activity of the enzyme. Exchanging the heme-anchoring cysteine group by a histidine exhibited promising behavior as the energy barriers decreased significantly. However, it is possible that the histidine modification also alters the reaction behavior of the peroxygenase, turning it into a peroxidase, an aspect that so far could not be confirmed beyond doubt. Simulations alone cannot conclusively determine whether substrate specificity and reactivity are maintained in the modifications tested. Nevertheless, our results highlight the importance of spin states and active pocket hydration for the catalytic reaction and demonstrate why a synergistic approach of theoretical predictions and experimental verifications is required for efficient enzyme engineering."},{"descriptionType":"Other","description":"15 pages, 7 figures, 1 table"}],"geoLocations":[],"fundingReferences":[],"url":"https://arxiv.org/abs/2606.21370","contentUrl":null,"metadataVersion":0,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2026-06-23T04:31:58Z","registered":"2026-06-23T04:31:59Z","published":null,"updated":"2026-06-23T04:31:59Z"},"relationships":{"client":{"data":{"id":"arxiv.content","type":"clients"}}}},{"id":"10.5445/ir/1000183762","type":"dois","attributes":{"doi":"10.5445/ir/1000183762","identifiers":[],"creators":[{"nameType":"Personal","affiliation":[],"givenName":"Niklas","familyName":"Teetz","name":"Teetz, Niklas","nameIdentifiers":[]},{"nameType":"Personal","affiliation":[],"givenName":"Luc","familyName":"Zuhse","name":"Zuhse, Luc","nameIdentifiers":[]},{"nameType":"Personal","affiliation":[],"givenName":"Dirk","familyName":"Holtmann","name":"Holtmann, Dirk","nameIdentifiers":[]}],"titles":[{"title":"Optimizing Yeast Surface-Displayed Unspecific Peroxygenase Production for Sustainable Biocatalysis"}],"publisher":"MDPI","container":{},"publicationYear":2025,"subjects":[],"contributors":[],"dates":[{"date":"2025","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"ScholarlyArticle","resourceTypeGeneral":"Text","citeproc":"article-journal","bibtex":"article","ris":"JOUR","resourceType":"Journal Article"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":["PDF"],"version":null,"rightsList":[{"rightsUri":"info:eu-repo/semantics/openAccess","rights":"Open Access"},{"rightsUri":"https://creativecommons.org/licenses/by/4.0/deed.de","rights":"Creative Commons Namensnennung 4.0 International"}],"descriptions":[],"geoLocations":[],"fundingReferences":[],"url":"https://publikationen.bibliothek.kit.edu/1000183762","contentUrl":null,"metadataVersion":1,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2025-08-04T09:26:22Z","registered":"2025-08-04T09:26:22Z","published":null,"updated":"2026-06-18T08:36:56Z"},"relationships":{"client":{"data":{"id":"tib.kit","type":"clients"}}}},{"id":"10.5526/err-00043369","type":"dois","attributes":{"doi":"10.5526/err-00043369","identifiers":[],"creators":[{"nameType":"Personal","givenName":"Harry","familyName":"Lang","name":"Lang, Harry","affiliation":[],"nameIdentifiers":[]}],"titles":[{"lang":"en","title":"Protein engineering of a cytochrome P450 decarboxylase from Jeotgalicoccus sp. ATCC 8456: structural, spectroscopic and kinetic studies"}],"publisher":"University of Essex","container":{},"publicationYear":2026,"subjects":[],"contributors":[],"dates":[{"date":"2026","dateType":"Issued"}],"language":null,"types":{"schemaOrg":"Thesis","resourceTypeGeneral":"Dissertation","citeproc":"thesis","bibtex":"phdthesis","ris":"THES","resourceType":"Thesis"},"relatedIdentifiers":[],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[],"descriptions":[{"descriptionType":"Abstract","description":"The bacterial cytochrome P450 peroxygenase family (CYP152) represents a unique class of heme-containing monooxygenases that utilise hydrogen peroxide as an oxidant, bypassing the canonical P450 redox partner system. Members of this family, particularly OleTJE, originally isolated from Jeotgalicoccus sp. ATCC 8456, are capable of catalysing oxidative decarboxylation of fatty acids to produce terminal alkenes (olefins). These olefins are of growing industrial interest as potential drop-in biofuels. The key reactive intermediate in this catalytic cycle is the ferryl-oxo porphyrin π-cation radical, commonly referred to as Compound I. However, due to its high reactivity and transient nature, direct characterisation of Compound I remains a significant challenge. This study focuses on engineering the hydrogen-bonding network surrounding the heme-b prosthetic group in OleTJE through site-directed mutagenesis, with the aim of extending the lifetime of Compound I. A combination of structural, kinetic, and spectroscopic techniques was employed to characterise the impact of these mutations. Fatty acid binding titrations revealed altered binding affinities through dissociation constants, stopped-flow UV/Vis spectrophotometry indicated a significant reduction in Compound I decay rate, and high-resolution macromolecular crystallography provided structural insights into the modified active site architecture. Future studies will incorporate techniques such as electron paramagnetic resonance (EPR) spectroscopy to investigate changes in the heme iron spin state equilibrium, offering deeper mechanistic insight into how these mutations influence the electronic environment of the active site as well as GC-MS analysis to confirm product formation and fatty acid presence post-purification. Collectively, these results demonstrate the potential of rational protein engineering to stabilise reactive intermediates and enhance enzymatic performance for biotechnological applications.","lang":"en"}],"geoLocations":[],"fundingReferences":[],"url":"http://repository.essex.ac.uk/id/eprint/43369","contentUrl":null,"metadataVersion":0,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2026-06-09T15:32:35Z","registered":"2026-06-09T15:32:36Z","published":null,"updated":"2026-06-09T15:32:36Z"},"relationships":{"client":{"data":{"id":"bl.essex","type":"clients"}}}},{"id":"10.24355/dbbs.084-202512101313-0","type":"dois","attributes":{"doi":"10.24355/dbbs.084-202512101313-0","identifiers":[{"identifier":"urn:nbn:de:gbv:084-2025121115010","identifierType":"URN"},{"identifier":"dbbs_mods_00079470","identifierType":"MyCoRe"}],"creators":[{"nameType":"Personal","affiliation":["Institut für Biochemie, Biotechnologie und Bioinformatik"],"givenName":"Margarita","familyName":"Seeger","name":"Seeger, Margarita","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0002-5609-6844"}]}],"titles":[{"lang":"en","title":"Computational and experimental studies on lignin converting enzymes"},{"titleType":"TranslatedTitle","lang":"de","title":"Computergestützte und experimentelle Studien zu Lignin-umwandelnden Enzymen"}],"publisher":"Universitätsbibliothek Braunschweig","container":{},"publicationYear":2025,"subjects":[{"subject":"570","subjectScheme":"ddc"}],"contributors":[{"nameType":"Organizational","affiliation":[],"name":"Universitätsbibliothek Braunschweig","nameIdentifiers":[],"contributorType":"HostingInstitution"},{"nameType":"Personal","givenName":"Anett","familyName":"Schallmey","name":"Schallmey, Anett","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0002-6670-0574"},{"nameIdentifierScheme":"GND","nameIdentifier":"1084786044"}],"contributorType":"Supervisor","affiliation":[]},{"nameType":"Personal","givenName":"Rebekka","familyName":"Biedendieck","name":"Biedendieck, Rebekka","nameIdentifiers":[{"nameIdentifierScheme":"ORCID","schemeUri":"https://orcid.org","nameIdentifier":"https://orcid.org/0000-0002-3567-6196"},{"nameIdentifierScheme":"GND","nameIdentifier":"132683598"}],"contributorType":"Supervisor","affiliation":[]}],"dates":[{"date":"2025-12-11","dateType":"Issued"}],"language":"en","types":{"schemaOrg":"Thesis","resourceTypeGeneral":"Text","citeproc":"thesis","bibtex":"phdthesis","ris":"THES","resourceType":"dissertation"},"relatedIdentifiers":[{"relationType":"HasMetadata","schemeUri":"https://www.loc.gov/standards/mods/v3/mods-3-7.xsd","relatedIdentifier":"https://leopard.tu-braunschweig.de/receive/dbbs_mods_00079470?XSL.Transformer=mods","relatedIdentifierType":"URL","relatedMetadataScheme":"mods"}],"relatedItems":[],"sizes":[],"formats":[],"version":null,"rightsList":[{"rightsIdentifierScheme":"SPDX","rightsUri":"https://creativecommons.org/licenses/by/4.0/legalcode","schemeUri":"https://spdx.org/licenses/","rights":"Creative Commons Attribution 4.0 International","lang":"en","rightsIdentifier":"cc-by-4.0"}],"descriptions":[{"descriptionType":"Abstract","description":"As a component of lignocellulose, lignin is one of the most abundant aromatic polymers on Earth. Its utilization is therefore considered a valuable alternative to the synthesis of aromatics from mineral oil. Glutathione-dependent β-etherases can cleave β-O-4 aryl ether bonds, which are the most common type of bond found in lignin. Due to their non-radical mechanism, these enzymes show promise as biocatalysts for the selective depolymerization of lignin polymers and oligomers, and for the production of aromatic platform chemicals from renewable raw materials. The first part of this work focused on investigating the catalytic mechanism of β-etherases and identifying important amino acid residues in the active site. Using computer-aided methods, various substrates were first docked into the active site of LigE and LigF, which then served as starting structures for molecular dynamics simulations. During the simulation, parameters were monitored that enabled a nucleophilic attack of the co-substrate glutathione on the beta-carbon of the substrate. For LigF, it was shown that the nucleophilic attack can take place. In addition, those amino acids that interact with the substrate during the simulation were experimentally subjected to an alanine scan in order to estimate the influence of the individual amino acids. Kinetic studies showed that the amino acids W115 and W148 are essential for catalysis, while S111, which is involved in the protonation of the leaving group, is of great importance but not essential. In addition, the simulation revealed a flexible helix-turn-helix motif, from which two proline residues were also replaced by alanine. The substitution of residue P142 led to significantly increased activity, probably due to the influence of increased movement of the domain. Also, LigE was investigated for its catalytic key residues. The results revealed that the crystal structure of LigE corresponds to a catalytic inactive form of the enzyme due to a truncation of 27 amino acids at the C-terminus. The second part of this thesis focused on heterologous production of unspecific peroxygenases and their potential role in lignin degradation. First, the expression of different potential peroxygenase genes in N. crassa and E. coli was investigated. No UPOs could be produced using the N. crassa production system. The situation was different for E. coli. With the help of co-produced chaperones, the short-type UPO from Botryobasidium botryosum could be produced in E. coli. Subsequent biochemical characterization of BboUPO revealed that this enzyme can catalyze numerous reactions and function over a wide pH range. Furthermore, BboUPO tolerates solvents such as acetonitrile and acetone up to a concentration of 10%. Due to its relatively large active site, BboUPO presumably prefers larger substrates than the typical UPO model substrates Finally, the involvement of UPOs in lignin depolymerization was investigated. The tested UPOs were examined using both lignin model substrates and a lignin oligomer mixture. The results showed that UPOs both demethylate and hydroxylate the model substrates. Lignin oligomers were also converted by UPOs to a certain extent, but this did not correspond to depolymerization. Future studies could combine UPOs with other lignin-degrading enzymes to contribute to the valorization of lignin.","lang":"en"},{"descriptionType":"Abstract","description":"Lignin ist ein Bestandteil von Lignocellulose und zählt zu den am häufigsten vorkommenden aromatischen Polymeren auf der Erde. Es gilt als alternative Quelle für aromatische Verbindungen, die sonst aus Mineralöl gewonnen werden. Glutathion-abhängige β-Etherasen können die in Lignin vorkommende β-O-4-Aryletherbindung spalten. Aufgrund ihres nicht-radikalen Reaktionsmechanismus sind diese Enzyme vielversprechende Biokatalysatoren für die selektive Depolymerisation von Ligninpolymeren und -oligomeren sowie für die Herstellung aromatischer Plattformchemikalien aus nachwachsenden Rohstoffen. Der erste Teil dieser Arbeit konzentrierte sich auf die Untersuchung des katalytischen Mechanismus von β-Etherasen und die Identifizierung wichtiger Aminosäurereste im aktiven Zentrum. Mithilfe computergestützter Methoden wurden zunächst verschiedene Substratstrukturen in das aktive Zentrum von LigE und LigF gedockt. Diese dienten dann als Ausgangsstrukturen für molekulardynamische Simulationen. Für LigF konnte gezeigt werden, dass ein nukleophiler Angriff durch das Co-Substrat Glutathion stattfinden kann. Darüber hinaus wurden diejenigen Aminosäuren, die während der Simulation mit dem Substrat interagierten, einem Alaninscan unterzogen, um den Einfluss der einzelnen Aminosäuren abzuschätzen. Kinetische Unter-suchungen zeigten, dass die Aminosäuren W115 und W148 für die Katalyse essenziell sind, während S111, welches an der Protonierung der Abgangsgruppe des Substrates beteiligt ist, zwar von großer, aber nicht von essenzieller Bedeutung ist. Darüber hinaus ergab die Simulation ein flexibles Helix-Turn-Helix-Motiv, bei dem ebenfalls zwei Prolinreste durch Alanin ersetzt wurden. Die Substitution des Restes P142 führte zu einer deutlich erhöhten Aktivität, was auf die erhöhte Flexibilität der Domäne zurückzuführen ist. Auch LigE wurde auf seine katalytischen Schlüsselreste untersucht. Die Ergebnisse zeigten, dass die Kristallstruktur von LigE aufgrund einer Verkürzung um 27 Aminosäuren am C-Terminus einer katalytisch inaktiven Form des Enzyms entspricht. Der zweite Teil dieser Arbeit konzentrierte sich auf die heterologe Produktion unspezifischer Peroxygenasen (UPO) und ihre potenzielle Rolle beim Ligninabbau. Zunächst wurde die Expression verschiedener potenzieller Peroxygenasegene in N. crassa und E. coli untersucht. Während mit dem N. crassa-Produktionssystem keine UPOs hergestellt werden konnten, konnte die kurze BboUPO aus Botryobasidium botryosum in E. coli, mithilfe von co-produzierten Chaperonen, löslich produziert werden. Die anschließende biochemische Charakterisierung von BboUPO ergab, dass dieses Enzym zahlreiche Reaktionen katalysieren kann und über einen breiten pH-Bereich hinweg aktiv ist. Darüber hinaus toleriert BboUPO Lösungsmittel wie Acetonitril und Aceton bis zu einer Konzentration von 10%. Schließlich wurde die Beteiligung von UPOs an der Depolymerisation von Lignin untersucht. Hierzu wurden die getesteten UPOs auf den Umsatz von Lignin-Modellsubstraten und einer Lignin-Oligomermischung untersucht. Die Ergebnisse zeigten, dass UPOs die Modellsubstrate sowohl demethylieren als auch hydroxylieren. Auch Lignin-Oligomere wurden durch UPOs umgewandelt, jedoch nicht depolymerisiert.","lang":"de"}],"geoLocations":[],"fundingReferences":[],"url":"https://leopard.tu-braunschweig.de/receive/dbbs_mods_00079470","contentUrl":null,"metadataVersion":1,"schemaVersion":"http://datacite.org/schema/kernel-4","source":"mds","isActive":true,"state":"findable","reason":null,"viewCount":0,"downloadCount":0,"referenceCount":0,"citationCount":0,"partCount":0,"partOfCount":0,"versionCount":0,"versionOfCount":0,"created":"2025-12-11T14:01:35Z","registered":"2025-12-11T14:01:36Z","published":null,"updated":"2026-06-04T22:12:00Z"},"relationships":{"client":{"data":{"id":"tib.ubbs","type":"clients"}}}}],"meta":{"total":178,"totalPages":8,"page":1},"links":{"self":"https://api.datacite.org/dois?query=peroxygenase","next":"https://api.datacite.org/dois?page%5Bnumber%5D=2\u0026page%5Bsize%5D=25\u0026query=peroxygenase"}}