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)
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publications
Total records: 126
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[ 2014 ] Pita M, Maté D, González-Pérez D, Shleev S, Fernández VM, Alcalde M, De Lacey AL Bioelectrochemical Oxidation of Water J. Am. Chem. Soc., 136: 5892-5895
[ 2014 ] Piumi F, Levasseur A, Navarro D, Zhou S, Macellaro G, Mathieu Y, Ropartz D, Ludwig R, Faulds CB, Record E A novel glucose dehydrogenase from the white-rot fungus Pycnoporus cinnabarinus: production in Aspergillus niger and physicochemical characterization of the recombinant enzyme. Appl. Microbiol. Biotechnol., 98: 10105-10118
[ 2014 ] Rico A, Rencoret J, del Río JC, Martínez AT, Gutiérrez A Pretreatment with laccase and a phenolic mediator degrades lignin and enhances saccharification of Eucalyptus feedstock Biotechnol. Biofuels, 7: 6
[ 2013 ] Babot ED, del Río JC, Kalum L, Martínez AT, Gutiérrez A Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from Coprinopsis cinerea Biotechnol. Bioeng., 110: 2323-2332
[ 2013 ] Bey M, Zhou S, Poidevin L, Henrissat B, Coutinho PM, Berrin JG, Sigoillot JC Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina Appl. Environ. Microbiol., 79: 488-496
[ 2013 ] Carabajal M, Kellner H, Levin L, Jehmlich N, Hofrichter M, Ullrich R The secretome of Trametes versicolor grown on tomato juice medium and purification of the secreted oxidoreductases including a versatile peroxidase J. Biotech., 168: 15-23
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.
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