Optimized oxidoreductases for medium and large scale industrial biotransformations
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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
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publications
Total records: 126
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[ 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
year2015
Oxidation and nitration of mononitrophenols by a DyP-type peroxidase
Büttner E, Ullrich R, Strittmatter E, Piontek K, Plattner D, Hofrichter M, Liers C
Arch. Biochem. Biophys., 574: 86-92

Substantial conversion of nitrophenols, typical high-redox potential phenolic substrates, by heme peroxidases has only been reported for lignin peroxidase (LiP) so far. But also a dye-decolorizing peroxidase of Auricularia auricula-judae (AauDyP) was found to be capable of acting on (i) ortho-nitrophenol (oNP), (ii) meta-nitrophenol (mNP) and (iii) para-nitrophenol (pNP). The pH dependency for pNP oxidation showed an optimum at pH 4.5, which is typical for phenol conversion by DyPs and other heme peroxidases. In the case of oNP and pNP conversion, dinitrophenols (2,4-DNP and 2,6-DNP) were identified as products and for pNP additionally p-benzoquinone. Moreover, indications were found for the formation of random polymerization products originating from initially formed phenoxy radical intermediates. Nitration was examined using 15N-labeled pNP and Na14NO2 as an additional source of nitro-groups. Products were identified by HPLC–MS, and mass-to-charge ratios were evaluated to clarify the origin of nitro-groups. The additional nitrogen in DNPs formed during enzymatic conversion was found to originate both from 15N-pNP and 14NO2Na. Based on these results, a hypothetical reaction scheme and a catalytically responsible confine of the enzyme’s active site are postulated.

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