Oxidoreductases on their way to industrial biotransformations
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...
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| Published in | Biotechnology advances Vol. 35; no. 6; pp. 815 - 831 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article Publication |
| Language | English |
| Published |
England
Elsevier Inc
01.11.2017
Elsevier Science Ltd Elsevier |
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| Online Access | Get full text |
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| Abstract | 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.
•Recent advances on fungal oxidoreductases for a bio-based economy are reviewed.•These include computer-aided rational design and directed evolution of biocatalysts.•Classical oxidoreductases consist of peroxidases/oxidases involved in lignin decay.•Peroxygenases and polysaccharide monooxygenases were more recently discovered.•Reviewed transformations consider both oxyfunctionalization and oxidation reactions. |
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| AbstractList | 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.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. 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. This work has been funded by the INDOX European project (KBBE-2013-7-613549), together with the BIO2014-56388-R and AGL2014-53730-R projects of the Spanish Ministry of Economy and Competitiveness (MINECO) co-financed by FEDER funds, and the BBI JU project EnzOx2 (H2020-BBI-PPP-2015-2-720297). The work conducted by the US DOE JGI was supported by the Office of Science of the US DOE under contract number DE-AC02-05CH11231. The authors thank other members of their groups at CIB-CSIC, Novozymes, Technical University of Dresden, JenaBios, University of Naples Federico II, Setas Kimya Sanayy, Wageningen University & Research, Anaxomics, Chiracon, BOKU, Delft University of Technology, INRABBF, Biopolis, Cheminova, CLEA, Solvay, IRNAS-CSIC and ICP-CSIC for their significant contributions to the results presented. Peer Reviewed 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. 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. •Recent advances on fungal oxidoreductases for a bio-based economy are reviewed.•These include computer-aided rational design and directed evolution of biocatalysts.•Classical oxidoreductases consist of peroxidases/oxidases involved in lignin decay.•Peroxygenases and polysaccharide monooxygenases were more recently discovered.•Reviewed transformations consider both oxyfunctionalization and oxidation reactions. 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. owever, 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. 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 H O as the source of oxygen and final electron acceptor. Flavo-oxidases are involved in both lignin and cellulose decay generating H O that activates peroxidases and generates hydroxyl radical. The group of copper oxidoreductases also includes other H O 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 D , 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. |
| Author | Tortajada, Marta Hofrichter, Martin Kılıç, Sibel del Río, José C. Hollmann, Frank Gelo-Pujic, Mirjana Liers, Christiane Linde, Dolores Herold-Majumdar, Owik M. Guallar, Victor Ludwig, Roland Faulds, Craig B. van Berkel, Willem J.H. Piscitelli, Alessandra Pezzella, Cinzia Rencoret, Jorge Camarero, Susana Martínez, Angel T. Lucas, Maria Fátima Winckelmann, Ib Fernández-Fueyo, Elena Vind, Jesper Sener, Mehmet E. Gutiérrez, Ana Record, Eric Alcalde, Miguel Rasmussen, Jo-Anne Lund, Henrik Serrano, Ana Tovborg, Morten Scheibner, Katrin Ruiz-Dueñas, Francisco J. Sannia, Giovanni Ullrich, René Zuhse, Ralf |
| Author_xml | – sequence: 1 givenname: Angel T. surname: Martínez fullname: Martínez, Angel T. email: ATMartinez@cib.csic.es organization: Centro de Investigaciones Biológicas, CSIC, Madrid, Spain – sequence: 2 givenname: Francisco J. surname: Ruiz-Dueñas fullname: Ruiz-Dueñas, Francisco J. organization: Centro de Investigaciones Biológicas, CSIC, Madrid, Spain – sequence: 3 givenname: Susana surname: Camarero fullname: Camarero, Susana organization: Centro de Investigaciones Biológicas, CSIC, Madrid, Spain – sequence: 4 givenname: Ana surname: Serrano fullname: Serrano, Ana organization: Centro de Investigaciones Biológicas, CSIC, Madrid, Spain – sequence: 5 givenname: Dolores surname: Linde fullname: Linde, Dolores organization: Centro de Investigaciones Biológicas, CSIC, Madrid, Spain – sequence: 6 givenname: Henrik surname: Lund fullname: Lund, Henrik organization: Novozymes A/S, Bagsvaerd, Denmark – sequence: 7 givenname: Jesper surname: Vind fullname: Vind, Jesper organization: Novozymes A/S, Bagsvaerd, Denmark – sequence: 8 givenname: Morten surname: Tovborg fullname: Tovborg, Morten organization: Novozymes A/S, Bagsvaerd, Denmark – sequence: 9 givenname: Owik M. orcidid: 0000-0002-1052-4970 surname: Herold-Majumdar fullname: Herold-Majumdar, Owik M. organization: Novozymes A/S, Bagsvaerd, Denmark – sequence: 10 givenname: Martin surname: Hofrichter fullname: Hofrichter, Martin organization: Technische Universität Dresden, Zittau, Germany – sequence: 11 givenname: Christiane surname: Liers fullname: Liers, Christiane organization: Technische Universität Dresden, Zittau, Germany – sequence: 12 givenname: René surname: Ullrich fullname: Ullrich, René organization: Technische Universität Dresden, Zittau, Germany – sequence: 13 givenname: Katrin surname: Scheibner fullname: Scheibner, Katrin organization: JenaBios GmBH, Jena, Germany – sequence: 14 givenname: Giovanni orcidid: 0000-0002-7986-6223 surname: Sannia fullname: Sannia, Giovanni organization: Università degli Studi di Napoli Federico II, Naples, Italy – sequence: 15 givenname: Alessandra surname: Piscitelli fullname: Piscitelli, Alessandra organization: Università degli Studi di Napoli Federico II, Naples, Italy – sequence: 16 givenname: Cinzia surname: Pezzella fullname: Pezzella, Cinzia organization: Università degli Studi di Napoli Federico II, Naples, Italy – sequence: 17 givenname: Mehmet E. surname: Sener fullname: Sener, Mehmet E. organization: Setas Kimya Sanayi AS, Tekirdag, Turkey – sequence: 18 givenname: Sibel surname: Kılıç fullname: Kılıç, Sibel organization: Setas Kimya Sanayi AS, Tekirdag, Turkey – sequence: 19 givenname: Willem J.H. surname: van Berkel fullname: van Berkel, Willem J.H. organization: Wageningen University & Research, The Netherlands – sequence: 20 givenname: Victor surname: Guallar fullname: Guallar, Victor organization: Anaxomics, Barcelona, Spain – sequence: 21 givenname: Maria Fátima orcidid: 0000-0001-8672-9940 surname: Lucas fullname: Lucas, Maria Fátima organization: Anaxomics, Barcelona, Spain – sequence: 22 givenname: Ralf surname: Zuhse fullname: Zuhse, Ralf organization: Chiracon GmBH, Luckenwalde, Germany – sequence: 23 givenname: Roland surname: Ludwig fullname: Ludwig, Roland organization: University of Natural Resources and Life Sciences (BOKU), Vienna, Austria – sequence: 24 givenname: Frank surname: Hollmann fullname: Hollmann, Frank organization: Department of Biotechnology, Delft University of Technology, Delft, The Netherlands – sequence: 25 givenname: Elena surname: Fernández-Fueyo fullname: Fernández-Fueyo, Elena organization: Department of Biotechnology, Delft University of Technology, Delft, The Netherlands – sequence: 26 givenname: Eric surname: Record fullname: Record, Eric organization: Aix Marseille University, INRA, UMR 1163 Biodiversité et Biotechnologie Fongiques (BBF), Marseille, France – sequence: 27 givenname: Craig B. surname: Faulds fullname: Faulds, Craig B. organization: Aix Marseille University, INRA, UMR 1163 Biodiversité et Biotechnologie Fongiques (BBF), Marseille, France – sequence: 28 givenname: Marta surname: Tortajada fullname: Tortajada, Marta organization: Biopolis, Valencia, Spain – sequence: 29 givenname: Ib surname: Winckelmann fullname: Winckelmann, Ib organization: Cheminova A/S, Lemvig, Denmark – sequence: 30 givenname: Jo-Anne surname: Rasmussen fullname: Rasmussen, Jo-Anne organization: CLEA Technologies BV, Delft, The Netherlands – sequence: 31 givenname: Mirjana surname: Gelo-Pujic fullname: Gelo-Pujic, Mirjana organization: Solvay, Brussels, Belgium – sequence: 32 givenname: Ana surname: Gutiérrez fullname: Gutiérrez, Ana organization: Instituto de Recursos Naturales y Agrobiología de Sevilla, CSIC, Seville, Spain – sequence: 33 givenname: José C. orcidid: 0000-0002-3040-6787 surname: del Río fullname: del Río, José C. organization: Instituto de Recursos Naturales y Agrobiología de Sevilla, CSIC, Seville, Spain – sequence: 34 givenname: Jorge surname: Rencoret fullname: Rencoret, Jorge organization: Instituto de Recursos Naturales y Agrobiología de Sevilla, CSIC, Seville, Spain – sequence: 35 givenname: Miguel surname: Alcalde fullname: Alcalde, Miguel organization: Instituto de Catálisis y Petroleoquímica, CSIC, Madrid, Spain |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28624475$$D View this record in MEDLINE/PubMed https://hal.science/hal-01557216$$DView record in HAL |
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| Keywords | CRO Directed evolution DFF HTP LPMO VAO CDH GDH Oxidases and dehydrogenases PELE Enzyme cascades LiP UPO LRET Lytic polysaccharide monooxygenases GMC Selective oxyfunctionalization HMF AAD QM/MM P2O MnP AAO GOX NMR Heme peroxidases and peroxygenases Laccases Rational design MOX MCO Lignocellulose biorefinery DyP VP FDCA HSQC ABTS FFCA Biophysical and biochemical computational modeling CPK oxidase peroxyde oxidoréductase péroxydase peroxides oxydase production d'enzyme biotransformation dynamique computationnelle des fluides monooxygénase |
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| SubjectTerms | 1-naphthol 25-hydroxycholecalciferol active sites Alkanes Analysis Basidiomycota Biochemical computers Biodegradation Biomass Biophysical and biochemical computational modeling biorefining Biotransformation Breaking down catalytic activity cellulose Chemical reactions Chemical synthesis Computer simulation computer software Copper Crystalline cellulose Decoloring delignification Dinitrocresols - chemistry Directed evolution Disintegration drugs Dyes Electron transfer electrons Engineering Enginyeria biomèdica Enzims Enzyme activation Enzyme cascades Fungi Fungi - chemistry Fungi - enzymology heme Heme - chemistry Heme - genetics Heme peroxidases and peroxygenases Hydrogen peroxide Hydroxyl radicals Indigo laccase Laccase - chemistry Laccase - genetics Laccases Life Sciences lignin Lignin - chemistry Lignin - genetics Lignocellulose Lignocellulose biorefinery Lytic polysaccharide monooxygenases Metabolites Naphthol Oxidases and dehydrogenases Oxidation Oxidation-Reduction Oxidoreductases Oxidoreductases - chemistry Oxidoreductases - classification Oxidoreductases - genetics Oxigenases oxygen Oxygenation peroxidases Peroxidases - chemistry Peroxidases - genetics Polyanilines Polysaccharides proteins Rational design screening Selective oxyfunctionalization Selectivity Studies Substrates Àrees temàtiques de la UPC |
| Title | Oxidoreductases on their way to industrial biotransformations |
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