Optimized oxidoreductases for medium and large scale industrial biotransformations
Project Secretariat
Dr Marta Pérez-Boada
E-mail: MPBoada@cib.csic.es
Consejo Superior de Investigaciones Científicas (CSIC)
Biological Research Centre (CIB)
Calle Ramiro de Maeztu 9, E-28040 Madrid, Spain
Phone: 34 918373112
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Total records: 126
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[ 2013 ] Churakova E, Arends IWCE, Hollmann F Increasing the Productivity of Peroxidase-Catalyzed Oxyfunctionalization: A Case Study on the Potential of Two-Liquid-Phase Systems ChemCatChem, 5: 565-568
[ 2013 ] Hahn F, Ullrich R, Hofrichter M, Liers C Experimental approach to follow the spatiotemporal wood degradation in fungal microcosms Biotechnol. J., 8: 127-132
[ 2013 ] Karich A, Kluge M, Ullrich R, Hofrichter M Benzene oxygenation and oxidation by the peroxygenase of Agrocybe aegerita AMB Express, 3: 5-13
[ 2013 ] Kluge M, Ullrich R, Scheibner K, Hofrichter M Formation of naphthalene hydrates in the enzymatic conversion of 1,2-dihydronaphthalene by two fungal peroxygenases and subsequent naphthalene formation J. Mol. Cat. B, doi: 10.1016/j.molcatb.2013.08.017
[ 2013 ] Liers C, Aranda E, Strittmatter E, Piontek K, Plattner D, Zorn H, Ullrich R, Hofrichter M Phenol oxidation by DyP-type peroxidases in comparison to fungal and plant peroxidases J. Mol. Cat. B, doi: 10.1016/j.molcatb.2013.09.025
[ 2013 ] Liers C, Pecyna MJ, Kellner H, Worrich A, Zorn H, Steffen KT, Hofrichter M, Ullrich R Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases Appl. Microbiol. Biotechnol., 97: 5839-5849
Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan
Linde D, Ayuso-Fernández I, Ruiz-Dueñas FJ, Martínez AT
Arch. Biochem. Biophys., 668: 23-28

Dye-decolorizing peroxidase (DyP) from Auricularia auricula-judae and versatile peroxidase (VP) from Pleurotus eryngii oxidize the three mononitrophenol isomers. Both enzymes have been overexpressed in Escherichia coli and in vitro activated. Despite their very different three-dimensional structures, the nitrophenol oxidation site is located at a solvent-exposed aromatic residue in both DyP (Trp377) and VP (Trp164), as revealed by liquid chromatography coupled to mass spectrometry and kinetic analyses of nitrophenol oxidation by the native enzymes and their tryptophan-less variants (the latter showing 10–60 fold lower catalytic efficiencies).

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Official webpage of indox [ industrialoxidoreductases ]. Optimized oxidoreductases for medium and large scale industrial biotransformations. This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under Grant Agreement nº: FP7-KBBE-2013-7-613549. © indox 2013. Developed by garcíarincón