Optimized oxidoreductases for medium and large scale industrial biotransformations
Total records:
126
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[ 2015 ]
Bormann S, Gomez Baraibar A, Ni Y, Holtmann D, Hollmann F Specific oxyfunctionalisations catalysed by peroxygenases: opportunities, challenges and solutions
Catal. Sci. Technol., 5: 2038-2052
[ 2015 ]
Büttner E, Ullrich R, Strittmatter E, Piontek K, Plattner D, Hofrichter M, Liers C Oxidation and nitration of mononitrophenols by a DyP-type peroxidase
Arch. Biochem. Biophys., 574: 86-92
[ 2015 ]
Fernandez-Fueyo E, Linde D, Almendral D, López-Lucendo MF, Ruiz-Dueñas FJ, Martínez AT Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II)
Appl. Microbiol. Biotechnol., doi: 10.1007/s00253-015-6665-3
[ 2015 ]
Fernandez-Fueyo E, van Wingerden M, Renirie R, Wever R, Ni Y, Holtmann D, Hollmann F Chemoenzymatic Halogenation of Phenols by using the Haloperoxidase from Curvularia inaequalis
ChemCatChem, doi: 10.1002/cctc.201500862
[ 2015 ]
Ferreira P, Carro J, Serrano A, Martínez AT A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes
Mycologia, 107: 1105-1119
[ 2015 ]
Ferreira P, Hernández-Ortega A, Lucas F, Carro J, Herguedas B, Borrelli K, Guallar V, Martínez AT, Medina M Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
FEBS J., 282: 3091-3106
year2015
Exploring the Oxidation of Lignin-Derived Phenols by a Library of Laccase Mutants
Pardo I, Camarero S
Molecules, 20: 15929-15943
Saturation mutagenesis was performed over six residues delimiting the substrate binding pocket of a fungal laccase previously engineered in the lab. Mutant libraries were screened using sinapic acid as a model substrate, and those mutants presenting increased activity were selected for exploring the oxidation of lignin-derived phenols. The latter comprised a battery of phenolic compounds of interest due to their use as redox mediators or precursors of added-value products and their biological activity. The new laccase variants were investigated in a multi-screening assay and the structural determinants, at both the substrate and the protein level, for the oxidation of the different phenols are discussed. Laccase activity greatly varied only by changing one or two residues of the enzyme pocket. Our results suggest that once the redox potential threshold is surpassed, the contribution of the residues of the enzymatic pocket for substrate recognition and binding strongly influence the overall rate of the catalytic reaction.
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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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