Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2014 ]
Levasseur A, Lomascolo A, Chabrol O, Ruiz-Dueñas FJ, [...] , Martínez AT, [...] , Record E The genome of the white-rot fungus Pycnoporus cinnabarinus: a basidiomycete model with a versatile arsenal for lignocellulosic biomass breakdown
BMC Genomics, 15: 486
[ 2014 ]
Linde D, Coscolín C, Liers C, Hofrichter M, Martínez AT, Ruiz-Dueñas FJ Heterologous expression and physicochemical characterization of a fungal dye-decolorizing peroxidase from Auricularia auricula-judae
Protein Expr. Purif., 103: 28-37
[ 2014 ]
Macellaro G, Baratto MC, Piscitelli A, Pezzella C, Fabrizi de Biani F, Palmese A, Piumi F, Record E, Basosi R, Sannia G Effective mutations in a high redox potential laccase from Pleurotus ostreatus
Appl. Microbiol. Biotechnol., doi: 10.1007/s00253-013-5491-8
[ 2014 ]
Macellaro G, Pezzella C, Cicatiello P, Sannia G, Piscitelli A Fungal Laccases Degradation of Endocrine Disrupting Compounds
BioMed Research International, doi: 10.1155/2014/614038
[ 2014 ]
Martínez AT, Ruiz-Dueñas FJ, Gutiérrez A, del Río JC, Alcalde M, Liers C, Ullrich R, Hofrichter M, Scheibner K, Kalum L, Vind J, Lund H Search, engineering, and applications of new oxidative biocatalysts
Biofuels, Bioprod. Bioref., 8: 819-835
[ 2014 ]
Molina-Espeja P, García-Ruiz E, González-Pérez D, Ullrich R, Hofrichter M, Alcalde M Directed evolution of Unspecific Peroxygenase from Agrocybe aegerita
Appl. Environ. Microbiol., 80: 3496-3507
year2019
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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[ 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
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