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
Fax: 34 915360432
Mobile: 34 650080476
Private area


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 ] Ewing TA, Gygli G, van Berkel WJ A single loop is essential for the octamerisation of vanillyl alcohol oxidase FEBS J., doi: 10.1111/febs.13762
[ 2016 ] Fernandez-Fueyo E, Ni Y, Gomez Baraibar A, Alcalde M, van Langen LM, Hollmann F Towards preparative peroxygenase-catalyzed oxyfunctionalization reactions in organic media J. Mol. Cat. B, doi: 10.1016/j.molcatb.2016.09.013
[ 2016 ] Fernandez-Fueyo E, Ruiz-Dueñas FJ, López-Lucendo MF, Pérez-Boada M, Rencoret J, Gutiérrez A, Pisabarro AG, Ramírez L, Martínez AT A secretomic view of woody and nonwoody lignocellulose degradation by Pleurotus ostreatus Biotechnol. Biofuels, 9: 49
[ 2016 ] Fernandez-Fueyo E, Younes SHH, van Rootselaar S, Aben RWM, Renirie R, Wever R, Holtmann D, Rutjes FPJT, Hollmann F A Biocatalytic Aza-Achmatowicz Reaction ACS-Catalysis, 6: 5904-5907
[ 2016 ] Garajova S, Mathieu Y, Beccia MR, Bennati-Granier C, Biaso F, Fanuel M, Ropartz D, Guigliarelli B, Record E, Rogniaux H, Henrissat B, Berrin JG Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose Sci. Rep., 6: 28276
[ 2016 ] González-Pérez D, Mateljak I, García-Ruiz E, Ruiz-Dueñas FJ, Martínez AT, Alcalde M Alkaline versatile peroxidase by directed evolution Catal. Sci. Technol., 6: 6625-6636
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