Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2014 ]
Levasseur A, Lomascolo A, Chabrol O, Ruiz-Dueñas FJ, [...] , Martínez AT, [...] , Record E The genome of the white-rot fungus Pycnoporus cinnabarinus: a basidiomycete model with a versatile arsenal for lignocellulosic biomass breakdown
BMC Genomics, 15: 486
[ 2014 ]
Linde D, Coscolín C, Liers C, Hofrichter M, Martínez AT, Ruiz-Dueñas FJ Heterologous expression and physicochemical characterization of a fungal dye-decolorizing peroxidase from Auricularia auricula-judae
Protein Expr. Purif., 103: 28-37
[ 2014 ]
Macellaro G, Baratto MC, Piscitelli A, Pezzella C, Fabrizi de Biani F, Palmese A, Piumi F, Record E, Basosi R, Sannia G Effective mutations in a high redox potential laccase from Pleurotus ostreatus
Appl. Microbiol. Biotechnol., doi: 10.1007/s00253-013-5491-8
[ 2014 ]
Macellaro G, Pezzella C, Cicatiello P, Sannia G, Piscitelli A Fungal Laccases Degradation of Endocrine Disrupting Compounds
BioMed Research International, doi: 10.1155/2014/614038
[ 2014 ]
Martínez AT, Ruiz-Dueñas FJ, Gutiérrez A, del Río JC, Alcalde M, Liers C, Ullrich R, Hofrichter M, Scheibner K, Kalum L, Vind J, Lund H Search, engineering, and applications of new oxidative biocatalysts
Biofuels, Bioprod. Bioref., 8: 819-835
[ 2014 ]
Molina-Espeja P, García-Ruiz E, González-Pérez D, Ullrich R, Hofrichter M, Alcalde M Directed evolution of Unspecific Peroxygenase from Agrocybe aegerita
Appl. Environ. Microbiol., 80: 3496-3507
year2013
Phenol oxidation by DyP-type peroxidases in comparison to fungal and plant peroxidases
Liers C, Aranda E, Strittmatter E, Piontek K, Plattner D, Zorn H, Ullrich R, Hofrichter M
J. Mol. Cat. B, doi: 10.1016/j.molcatb.2013.09.025
Over the last years, novel peroxidases secreted by lignocellulose-degrading agaricomycetes have been discovered. Among them, the so-called DyP-type peroxidases (DyPs) that are secreted under conditions close to nature (i.e. in wood cultures) are of particular interest, since they are able to oxidize diverse substrates including veratryl alcohol, non-phenolic lignin model dimers as well as recalcitrant phenols and dyes. In spite of their unique protein structure and their catalytic versatility, the estimation of the redox potential of this new peroxidase group is still pending. To solve this problem, we used a catalytic approach developed by Ayala et al., 2007 [21], which is based on the Marcus equation and the determination of the redox thermodynamics between heme-peroxidase compound II and the resting state enzyme. Five fungal DyPs (among them four wild-type enzymes and one recombinant protein) were tested regarding phenol oxidation in comparison to other well-studied plant and fungal peroxidases (soybean peroxidase, SBP,Coprinopsis cinerea peroxidase, CiP, lignin peroxidase of Phanerochaete chrysosporium, LiP). DyP-type peroxidases have a high affinity for phenols and can oxidize even recalcitrant representatives such as p-nitrophenol. Based on this “phenol oxidation method”, their redox potential was estimated to range between 1.10 ± 0.02 and 1.20 ± 0.1 V, which is between the values calculated for high-redox potential LiP (1.26 ± 0.17 V) and low-redox potential, phenol-oxidizing plant (0.93 ± 0.04 V for SBP) and fungal (1.06 ± 0.07 V for CiP) peroxidases.
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[ 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
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