Optimized oxidoreductases for medium and large scale industrial biotransformations
Project Secretariat
Dr Marta Pérez-Boada
E-mail: MPBoada@cib.csic.esConsejo Superior de Investigaciones Científicas (CSIC)
Biological Research Centre (CIB)
Calle Ramiro de Maeztu 9, E-28040 Madrid, Spain
Phone: 34 918373112
Fax: 34 915360432
Mobile: 34 650080476
Private area
publications
Pages:
1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 
[ 2015 ]
Poraj-Kobielska M, Peter S, Leonhardt S, Ullrich R, Scheibner K, Hofrichter M Immobilization of unspecific peroxygenases (EC 1.11.2.1) in PVA/PEG gel and hollow fiber modules
Biochem. Eng. J., 98: 144-150
[ 2015 ]
Rico A, Rencoret J, del Río JC, Martínez AT, Gutiérrez A In-Depth 2D NMR Study of Lignin Modification During Pretreatment of Eucalyptus Wood with Laccase and Mediators
Bioenerg. Res., 8: 211-230
[ 2015 ]
Saez-Jimenez V, Acebes S, Guallar V, Martínez AT, Ruiz-Dueñas FJ Improving the oxidative stability of a high redox potential fungal peroxidase by rational design
PlosOne, 10-4
[ 2015 ]
Saez-Jimenez V, Baratto MC, Pogni R, Rencoret J, Gutiérrez A, Santos JI, Martínez AT, Ruiz-Dueñas FJ Demonstration of Lignin-to-Peroxidase Direct Electron Transfer: A Transient-state Kinetics, Directed Mutagenesis, EPR and NMR Study
J. Biol. Chem., 290: 23201-23213
[ 2015 ]
Saez-Jimenez V, Fernandez-Fueyo E, Medrano FJ, Romero A, Martínez AT, Ruiz-Dueñas FJ Improving the pH-stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase
PlosOne, doi: 10.1371/journal.pone.0140984
[ 2015 ]
Tan TC, Kracher D, Gandini R, Sygmund C, Kittl R, Haltrich D, Hällberg BM, Ludwig R, Divine C Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation
Nat. Commun., 6: 7542
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
[ 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