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<export-example>
  <doc>
    <id>20670</id>
    <completedYear/>
    <publishedYear>2017</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>815</pageFirst>
    <pageLast>831</pageLast>
    <pageNumber/>
    <edition/>
    <issue>6</issue>
    <volume>35</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2017-12-01</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Oxidoreductases on their way to industrial biotransformations</title>
    <abstract language="eng">Fungi produce heme-containing peroxidases and peroxygenases, flavin-containing oxidases and dehydrogenases, and different copper-containing oxidoreductases involved in the biodegradation of lignin and other recalcitrant compounds. Heme peroxidases comprise the classical ligninolytic peroxidases and the new dye-decolorizing peroxidases, while heme peroxygenases belong to a still largely unexplored superfamily of heme-thiolate proteins. Nevertheless, basidiomycete unspecific peroxygenases have the highest biotechnological interest due to their ability to catalyze a variety of regio- and stereo-selective monooxygenation reactions with H2O2 as the source of oxygen and final electron acceptor. Flavo-oxidases are involved in both lignin and cellulose decay generating H2O2 that activates peroxidases and generates hydroxyl radical. The group of copper oxidoreductases also includes other H2O2 generating enzymes - copper-radical oxidases - together with classical laccases that are the oxidoreductases with the largest number of reported applications to date. However, the recently described lytic polysaccharide monooxygenases have attracted the highest attention among copper oxidoreductases, since they are capable of oxidatively breaking down crystalline cellulose, the disintegration of which is still a major bottleneck in lignocellulose biorefineries, along with lignin degradation. Interestingly, some flavin-containing dehydrogenases also play a key role in cellulose breakdown by directly/indirectly “fueling” electrons for polysaccharide monooxygenase activation. Many of the above oxidoreductases have been engineered, combining rational and computational design with directed evolution, to attain the selectivity, catalytic efficiency and stability properties required for their industrial utilization. Indeed, using ad hoc software and current computational capabilities, it is now possible to predict substrate access to the active site in biophysical simulations, and electron transfer efficiency in biochemical simulations, reducing in orders of magnitude the time of experimental work in oxidoreductase screening and engineering. What has been set out above is illustrated by a series of remarkable oxyfunctionalization and oxidation reactions developed in the frame of an intersectorial and multidisciplinary European RTD project. The optimized reactions include enzymatic synthesis of 1-naphthol, 25-hydroxyvitamin D3, drug metabolites, furandicarboxylic acid, indigo and other dyes, and conductive polyaniline, terminal oxygenation of alkanes, biomass delignification and lignin oxidation, among others. These successful case stories demonstrate the unexploited potential of oxidoreductases in medium and large-scale biotransformations.</abstract>
    <parentTitle language="eng">Biotechnology Advances</parentTitle>
    <identifier type="doi">10.1016/j.biotechadv.2017.06.003</identifier>
    <identifier type="issn">1873-1899</identifier>
    <identifier type="issn">0734-9750</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <author>
      <firstName>Angel T.</firstName>
      <lastName>Martinez</lastName>
    </author>
    <submitter>
      <firstName>Kai-Uwe</firstName>
      <lastName>Schmidtke</lastName>
    </submitter>
    <author>
      <firstName>Francisco J.</firstName>
      <lastName>Ruiz-Duenas</lastName>
    </author>
    <author>
      <firstName>Susana</firstName>
      <lastName>Camarero</lastName>
    </author>
    <author>
      <firstName>Ana</firstName>
      <lastName>Serrano</lastName>
    </author>
    <author>
      <firstName>Dolores</firstName>
      <lastName>Linde</lastName>
    </author>
    <author>
      <firstName>Henrik</firstName>
      <lastName>Lund</lastName>
    </author>
    <author>
      <firstName>Jesper</firstName>
      <lastName>Vind</lastName>
    </author>
    <author>
      <firstName>Morton</firstName>
      <lastName>Tovborg</lastName>
    </author>
    <author>
      <firstName>Owik M.</firstName>
      <lastName>Herold-Majumdar</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Christiane</firstName>
      <lastName>Liers</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Giovanni</firstName>
      <lastName>Sannia</lastName>
    </author>
    <author>
      <firstName>Alessandra</firstName>
      <lastName>Piscitelli</lastName>
    </author>
    <author>
      <firstName>Mehmet E.</firstName>
      <lastName>Sener</lastName>
    </author>
    <author>
      <firstName>Sibel</firstName>
      <lastName>Kilic</lastName>
    </author>
    <author>
      <firstName>Willem J. H. van</firstName>
      <lastName>Berkel</lastName>
    </author>
    <author>
      <firstName>Víctor</firstName>
      <lastName>Guallar</lastName>
    </author>
    <author>
      <firstName>Maria Fátima</firstName>
      <lastName>Lucas</lastName>
    </author>
    <author>
      <firstName>Ralf</firstName>
      <lastName>Zuhse</lastName>
    </author>
    <author>
      <firstName>Roland</firstName>
      <lastName>Ludwig</lastName>
    </author>
    <author>
      <firstName>Frank</firstName>
      <lastName>Hollmann</lastName>
    </author>
    <author>
      <firstName>Elena</firstName>
      <lastName>Fernández-Fueyo</lastName>
    </author>
    <author>
      <firstName>Eric</firstName>
      <lastName>Record</lastName>
    </author>
    <author>
      <firstName>Craig B.</firstName>
      <lastName>Faulds</lastName>
    </author>
    <author>
      <firstName>Marta</firstName>
      <lastName>Tortajada</lastName>
    </author>
    <author>
      <firstName>Ib</firstName>
      <lastName>Winckelmann</lastName>
    </author>
    <author>
      <firstName>Jo-Anne</firstName>
      <lastName>Rasmussen</lastName>
    </author>
    <author>
      <firstName>Mirjana</firstName>
      <lastName>Gelo-Pujic</lastName>
    </author>
    <author>
      <firstName>Ana</firstName>
      <lastName>Gutiérrez</lastName>
    </author>
    <author>
      <firstName>José C. del</firstName>
      <lastName>Rio</lastName>
    </author>
    <author>
      <firstName>Jorge</firstName>
      <lastName>Rencoret</lastName>
    </author>
    <author>
      <firstName>Miguel</firstName>
      <lastName>Alcalde</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Biotechnology</value>
    </subject>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>20669</id>
    <completedYear/>
    <publishedYear>2017</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>16989</pageFirst>
    <pageLast>67</pageLast>
    <pageNumber>16985</pageNumber>
    <edition/>
    <issue/>
    <volume>23</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2017-12-01</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Fatty Acid Chain Shortening by a Fungal Peroxygenase</title>
    <abstract language="eng">A recently discovered peroxygenase from the&#13;
fungus Marasmius rotula (MroUPO) is able to catalyze the&#13;
progressive one-carbon shortening of medium and longchain mono- and dicarboxylic acids by itself alone, in the presence of H₂O₂. The mechanism, analyzed using H₂O, starts with an a-oxidation catalyzed by MroUPO generat- ing an α-hydroxy acid, which is further oxidized by the enzyme to a reactive α-keto intermediate whose decarboxylation yields the one-carbon shorter fatty acid. Compared with the previously characterized peroxygenase of Agrocybe aegerita, a wider heme access channel, enabling fatty acid positioning with the carboxylic end near the heme cofactor (as seen in one of the crystal structures available) could be at the origin of the unique ability of MroUPO shortening carboxylic acid chains.</abstract>
    <parentTitle language="eng">Chemistry A European Journal</parentTitle>
    <identifier type="doi">10.1002/chem.201704773</identifier>
    <identifier type="issn">1521-3765</identifier>
    <identifier type="issn">0947-6539</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <enrichment key="review.accepted_by">2</enrichment>
    <author>
      <firstName>Andrés</firstName>
      <lastName>Olmedo</lastName>
    </author>
    <submitter>
      <firstName>Kai-Uwe</firstName>
      <lastName>Schmidtke</lastName>
    </submitter>
    <author>
      <firstName>José C. del</firstName>
      <lastName>Río</lastName>
    </author>
    <author>
      <firstName>Jan</firstName>
      <lastName>Kiebist</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Angel T.</firstName>
      <lastName>Martínez</lastName>
    </author>
    <author>
      <firstName>Ana</firstName>
      <lastName>Gutiérrez</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>22916</id>
    <completedYear/>
    <publishedYear>2018</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>2394</pageFirst>
    <pageLast>2401</pageLast>
    <pageNumber/>
    <edition/>
    <issue>8</issue>
    <volume>9</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2018-12-18</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Selective synthesis of the resveratrol analogue 4,4′-dihydroxy-trans-stilbene and stilbenoids modification by fungal peroxygenases</title>
    <abstract language="eng">This work gives first evidence that the unspecific peroxygenases (UPOs) from the basidiomycetes Agrocybe aegerita (AaeUPO), Coprinopsis cinerea (rCciUPO) and Marasmius rotula (MroUPO) are able to catalyze the regioselective hydroxylation of trans-stilbene to 4,4′-dihydroxy-trans-stilbene (DHS), a resveratrol (RSV) analogue whose preventive effects on cancer invasion and metastasis have very recently been shown. Nearly complete transformation of substrate (yielding DHS) was achieved with the three enzymes tested, using H2O2 as the only co-substrate, with AaeUPO showing exceptionally higher total turnover number (200 000) than MroUPO (26 000) and rCciUPO (1400). Kinetic studies demonstrated that AaeUPO was the most efficient enzyme catalyzing stilbene dihydroxylation with catalytic efficiencies (kcat/Km) one and two orders of magnitude higher than those of MroUPO and rCciUPO, so that 4-hydroxystilbene appears to be the best UPO substrate reported to date. In contrast, the peroxygenase from the ascomycete Chaetomium globosum (CglUPO) failed to hydroxylate trans-stilbene at the aromatic ring and instead produced the trans-epoxide in the alkenyl moiety. In addition, stilbenoids such as pinosylvin (Pin) and RSV were tested as substrates for the enzymatic synthesis of RSV from Pin and oxyresveratrol (oxyRSV) from both RSV and Pin. Overall, lower conversion rates and regioselectivities compared with trans-stilbene were accomplished by three of the UPOs, and no conversion was observed with CglUPO. The highest amount of RSV (63% of products) and oxyRSV (78%) were again attained with AaeUPO. True peroxygenase activity was demonstrated by incorporation of 18O from H218O2 into the stilbene hydroxylation products. Differences in the number of phenylalanine residues at the heme access channels seems related to differences in aromatic hydroxylation activity, since they would facilitate substrate positioning by aromatic-aromatic interactions. The only ascomycete UPO tested (that of C. globosum) turned out to have the most differing active site (distal side of heme cavity) and reactivity with stilbenes resulting in ethenyl epoxidation instead of aromatic hydroxylation. The above oxyfunctionalizations by fungal UPOs represent a novel and simple alternative to chemical synthesis for the production of DHS, RSV and oxyRSV.</abstract>
    <parentTitle language="eng">Catalysis Science &amp; Technology</parentTitle>
    <identifier type="doi">10.1039/C8CY00272J</identifier>
    <identifier type="issn">2044-4761</identifier>
    <identifier type="issn">2044-4753</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <author>
      <firstName>Carmen</firstName>
      <lastName>Aranda</lastName>
    </author>
    <submitter>
      <firstName>Kai-Uwe</firstName>
      <lastName>Schmidtke</lastName>
    </submitter>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Jan</firstName>
      <lastName>Kiebist</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>José C. del</firstName>
      <lastName>Río</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Angel T.</firstName>
      <lastName>Martínez</lastName>
    </author>
    <author>
      <firstName>Ana</firstName>
      <lastName>Gutiérrez</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>22919</id>
    <completedYear/>
    <publishedYear>2018</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>3964</pageFirst>
    <pageLast>3968</pageLast>
    <pageNumber/>
    <edition/>
    <issue>18</issue>
    <volume>10</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2018-12-18</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Selective Epoxidation of Fatty Acids and Fatty Acid Methyl Esters by Fungal Peroxygenases</title>
    <abstract language="eng">Recently discovered fungal unspecific peroxygenases from Marasmius rotula and Chaetomium globosum catalyze the epoxidation of unsaturated fatty acids (FA) and FA methyl esters (FAME), unlike the well‐known peroxygenases from Agrocybe aegerita and Coprinopsis cinerea. Reactions of a series of unsaturated FA and FAME with cis‐configuration revealed high (up to 100 %) substrate conversion and selectivity towards epoxidation, although some significant differences were observed between enzymes and substrates with the best results being obtained with the C. globosum enzyme. This and the M. rotula peroxygenase appear as promising biocatalysts for the environmentally‐friendly production of reactive FA epoxides given their self‐sufficient monooxygenase activity and the high conversion rate and epoxidation selectivity.</abstract>
    <parentTitle language="eng">CHEMCATCHEM</parentTitle>
    <identifier type="doi">10.1002/cctc.201800849</identifier>
    <identifier type="issn">1867-3899</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <author>
      <firstName>Carmen</firstName>
      <lastName>Aranda</lastName>
    </author>
    <submitter>
      <firstName>Kai-Uwe</firstName>
      <lastName>Schmidtke</lastName>
    </submitter>
    <author>
      <firstName>Andrés</firstName>
      <lastName>Olmedo</lastName>
    </author>
    <author>
      <firstName>Jan</firstName>
      <lastName>Kiebist</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>José C. del</firstName>
      <lastName>Río</lastName>
    </author>
    <author>
      <firstName>Angel T.</firstName>
      <lastName>Martínez</lastName>
    </author>
    <author>
      <firstName>Ana</firstName>
      <lastName>Gutiérrez</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>28874</id>
    <completedYear/>
    <publishedYear>2022</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>1</pageFirst>
    <pageLast>12</pageLast>
    <pageNumber/>
    <edition/>
    <issue>3</issue>
    <volume>11</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation>Consejo Superior de Investigaciones Científicas (CSIC)</contributingCorporation>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2022-05-16</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Enzymatic Epoxidation of Long-Chain Terminal Alkenes by Fungal Peroxygenases</title>
    <abstract language="eng">Terminal alkenes are among the most attractive starting materials for the synthesis of epoxides, which are essential and versatile intermediate building blocks for the pharmaceutical, flavoring, and polymer industries. Previous research on alkene epoxidation has focused on the use of several oxidizing agents and/or different enzymes, including cytochrome P450 monooxygenases, as well as microbial whole-cell catalysts that have several drawbacks. Alternatively, we explored the ability of unspecific peroxygenases (UPOs) to selectively epoxidize terminal alkenes. UPOs are attractive biocatalysts because they are robust extracellular enzymes and only require H2O2 as cosubstrate. Here, we show how several UPOs, such as those from Cyclocybe (Agrocybe) aegerita (AaeUPO), Marasmius rotula (MroUPO), Coprinopsis cinerea (rCciUPO), Humicola insolens (rHinUPO), and Daldinia caldariorum (rDcaUPO), are able to catalyze the epoxidation of long-chain terminal alkenes (from C12:1 to C20:1) after an initial optimization of several reaction parameters (cosolvent, cosubstrate, and pH). In addition to terminal epoxides, alkenols and other hydroxylated derivatives of the alkenes were formed. Although all UPOs were able to convert and epoxidize the alkenes, notable differences were observed between them, with rCciUPO being responsible for the highest substrate turnover and MroUPO being the most selective with respect to terminal epoxidation. The potential of peroxygenases for epoxidizing long-chain terminal alkenes represents an interesting and green alternative to the existing synthesis technologies.</abstract>
    <parentTitle language="eng">Antioxidants</parentTitle>
    <identifier type="url">https://www.mdpi.com/2076-3921/11/3/522</identifier>
    <identifier type="doi">10.3390/antiox11030522</identifier>
    <identifier type="issn">2076-3921</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <enrichment key="Artikelnummer">522</enrichment>
    <enrichment key="opus.source">publish</enrichment>
    <enrichment key="opus.doi.autoCreate">false</enrichment>
    <enrichment key="opus.urn.autoCreate">false</enrichment>
    <enrichment key="Fprofil">2 Gesundheit und Lifes Sciences / Health and Life Sciences</enrichment>
    <author>
      <firstName>Esteban D.</firstName>
      <lastName>Babot</lastName>
    </author>
    <submitter>
      <firstName>Kai-Uwe</firstName>
      <lastName>Schmidtke</lastName>
    </submitter>
    <author>
      <firstName>Carmen</firstName>
      <lastName>Aranda</lastName>
    </author>
    <author>
      <firstName>Jan</firstName>
      <lastName>Kiebist</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Angel T.</firstName>
      <lastName>Martínez</lastName>
    </author>
    <author>
      <firstName>Ana</firstName>
      <lastName>Gutierrez</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>oxyfunctionalization</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>epoxidation</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>terminal alkenes</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>epoxides</value>
    </subject>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>36571</id>
    <completedYear/>
    <publishedYear>2023</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>1</pageFirst>
    <pageLast>9</pageLast>
    <pageNumber>9</pageNumber>
    <edition/>
    <issue>9</issue>
    <volume>62</volume>
    <type>articler</type>
    <publisherName>Wiley-VCH</publisherName>
    <publisherPlace>Weinheim</publisherPlace>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2025-10-14</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Engineering a highly regioselective fungal peroxygenase for the synthesis of hydroxy fatty acids</title>
    <abstract language="eng">The hydroxylation of fatty acids is an appealing reaction in synthetic chemistry, although the lack of selective catalysts hampers its industrial implementation. In this study, we have engineered a highly regioselective fungal peroxygenase for the ω-1 hydroxylation of fatty acids with quenched stepwise over-oxidation. One single mutation near the Phe catalytic tripod narrowed the heme cavity, promoting a dramatic shift toward subterminal hydroxylation with a drop in the over-oxidation activity. While crystallographic soaking experiments and molecular dynamic simulations shed light on this unique oxidation pattern, the selective biocatalyst was produced by Pichia pastoris at 0.4 g L−1 in a fed-batch bioreactor and used in the preparative synthesis of 1.4 g of (ω-1) hydroxytetradecanoic acid with 95 % regioselectivity and 83 % ee for the S enantiomer.</abstract>
    <parentTitle language="eng">Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker</parentTitle>
    <identifier type="doi">10.1002/anie.202217372</identifier>
    <identifier type="issn">1521-3773</identifier>
    <enrichment key="Fprofil">2 Gesundheit und Lifes Sciences / Health and Life Sciences</enrichment>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <enrichment key="Artikelnummer">62: e202217372</enrichment>
    <enrichment key="opus.source">publish</enrichment>
    <enrichment key="opus.doi.autoCreate">false</enrichment>
    <enrichment key="opus.urn.autoCreate">false</enrichment>
    <licence>Creative Commons - CC BY - Namensnennung 4.0 International</licence>
    <author>
      <firstName>Patricia</firstName>
      <lastName>Gomez de Santos</lastName>
    </author>
    <submitter>
      <firstName>Schmidtke</firstName>
      <lastName>Kai-Uwe</lastName>
    </submitter>
    <author>
      <firstName>Alejandro</firstName>
      <lastName>González-Benjumea</lastName>
    </author>
    <author>
      <firstName>Angela</firstName>
      <lastName>Fernandez-Garcia</lastName>
    </author>
    <author>
      <firstName>Carmen</firstName>
      <lastName>Aranda</lastName>
    </author>
    <author>
      <firstName>Yinqi</firstName>
      <lastName>Wu</lastName>
    </author>
    <author>
      <firstName>Andrada</firstName>
      <lastName>But</lastName>
    </author>
    <author>
      <firstName>Patricia</firstName>
      <lastName>Molina-Espeja</lastName>
    </author>
    <author>
      <firstName>Diana M.</firstName>
      <lastName>Maté</lastName>
    </author>
    <author>
      <firstName>David</firstName>
      <lastName>Gonzalez-Perez</lastName>
    </author>
    <author>
      <firstName>Wuyuan</firstName>
      <lastName>Zhang</lastName>
    </author>
    <author>
      <firstName>Jan</firstName>
      <lastName>Kiebist</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Katarzyna</firstName>
      <lastName>Swiderek</lastName>
    </author>
    <author>
      <firstName>Vicent</firstName>
      <lastName>Moliner</lastName>
    </author>
    <author>
      <firstName>Julia</firstName>
      <lastName>Sanz-Aparicio</lastName>
    </author>
    <author>
      <firstName>Frank</firstName>
      <lastName>Hollmann</lastName>
    </author>
    <author>
      <firstName>Ana</firstName>
      <lastName>Gutiérrez</lastName>
    </author>
    <author>
      <firstName>Miguel</firstName>
      <lastName>Alcalde</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
</export-example>
