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
Benzene oxygenation and oxidation by the peroxygenase of Agrocybe aegerita
Karich A, Kluge M, Ullrich R, Hofrichter M
AMB Express, 3: 5-13
Aromatic peroxygenase (APO) is an extracellular enzyme produced by the agaric basidiomycete Agrocybe aegerita that catalyzes diverse peroxide-dependent oxyfunctionalization reactions. Here we describe the oxygenation of the unactivated aromatic ring of benzene with hydrogen peroxide as co-substrate. The optimum pH of the reaction was around 7 and it proceeded via an initial epoxide intermediate that re-aromatized in aqueous solution to form phenol. Identity of the epoxide intermediate as benzene oxide was proved by a freshly prepared authentic standard using GC-MS and LC-MS analyses. Second and third [per]oxygenation was also observed and resulted in the formation of further hydroxylation and following [per]oxidation products: hydroquinone and p-benzoquinone, catechol and o-benzoquinone as well as 1,2,4-trihydroxybenzene and hydroxy-p-benzoquinone, respectively. Using H218O2 as co-substrate and ascorbic acid as radical scavenger, inhibiting the formation of peroxidation products (e.g., p-benzoquinone), the origin of the oxygen atom incorporated into benzene or phenol was proved to be the peroxide. Apparent enzyme kinetic constants (kcat, Km) for the peroxygenation of benzene were estimated to be around 8 s-1 and 3.6 mM. These results raise the possibility that peroxygenases may be useful for enzymatic syntheses of hydroxylated benzene derivatives under mild conditions.
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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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