Optimized oxidoreductases for medium and large scale industrial biotransformations
Total records:
126
Pages:
1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21
[ 2014 ]
Pita M, Maté D, González-Pérez D, Shleev S, Fernández VM, Alcalde M, De Lacey AL Bioelectrochemical Oxidation of Water
J. Am. Chem. Soc., 136: 5892-5895
[ 2014 ]
Piumi F, Levasseur A, Navarro D, Zhou S, Macellaro G, Mathieu Y, Ropartz D, Ludwig R, Faulds CB, Record E A novel glucose dehydrogenase from the white-rot fungus Pycnoporus cinnabarinus: production in Aspergillus niger and physicochemical characterization of the recombinant enzyme.
Appl. Microbiol. Biotechnol., 98: 10105-10118
[ 2014 ]
Rico A, Rencoret J, del Río JC, Martínez AT, Gutiérrez A Pretreatment with laccase and a phenolic mediator degrades lignin and enhances saccharification of Eucalyptus feedstock
Biotechnol. Biofuels, 7: 6
[ 2013 ]
Babot ED, del Río JC, Kalum L, Martínez AT, Gutiérrez A Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from Coprinopsis cinerea
Biotechnol. Bioeng., 110: 2323-2332
[ 2013 ]
Bey M, Zhou S, Poidevin L, Henrissat B, Coutinho PM, Berrin JG, Sigoillot JC Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina
Appl. Environ. Microbiol., 79: 488-496
[ 2013 ]
Carabajal M, Kellner H, Levin L, Jehmlich N, Hofrichter M, Ullrich R The secretome of Trametes versicolor grown on tomato juice medium and purification of the secreted oxidoreductases including a versatile peroxidase
J. Biotech., 168: 15-23
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).
Download the article for free until July 5th on: https://authors.elsevier.com/a/1Z3YPw0NEPWp
Official webpage of

[ 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