Optimized oxidoreductases for medium and large scale industrial biotransformations
CLOSE
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
Fax: 34 915360432
Mobile: 34 650080476
CLOSE
Private area
User:


Password:

publications
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  

[ 2016 ] Pardo I, Santiago G, Gentili P, Lucas F, Monza E, Medrano FJ, Galli C, Martínez AT, Guallar V, Camarero S Re-designing the substrate binding pocket of laccase for enhanced oxidation of sinapic acid Catal. Sci. Technol., doi: 10.1039/C5CY01725D
[ 2016 ] Rencoret J, Pereira A, del Río JC, Martínez AT, Gutiérrez A Laccase-Mediator Pretreatment of Wheat Straw Degrades Lignin and Improves Saccharification Bioenerg. Res., 9: 917-930
[ 2016 ] Saez-Jimenez V, Acebes S, García-Ruiz E, Romero A, Guallar V, Alcalde M, Medrano FJ, Martínez AT, Ruiz-Dueñas FJ Unveiling the basis of alkaline stability of an evolved versatile peroxidase Biochem. J., 473: 1917-1928
[ 2016 ] Saez-Jimenez V, Rencoret J, Rodríguez-Carvajal MA, Gutiérrez A, Ruiz-Dueñas FJ, Martínez AT Role of surface tryptophan for peroxidase oxidation of nonphenolic lignin Biotechnol. Biofuels, 9: 198-211
[ 2016 ] Salvachúa D, Katahira R, Cleveland NS, Khanna P, Resch MG, Black BA, Purvine SO, Zink EM, Prieto A, Martínez MJ, Martínez AT, Simmons BA, Gladden JM, Beckham GT Lignin depolymerization by fungal secretomes and a microbial sink Green Chem., doi: 10.1039/C6GC01531J
[ 2016 ] Santiago G, de Salas F, Lucas F, Monza E, Acebes S, Martínez AT, Camarero S, Guallar V Computer-Aided Laccase Engineering: Toward Biological Oxidation of Arylamines ACS-Catalysis, 6: 5415-5423
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 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