Optimized oxidoreductases for medium and large scale industrial biotransformations
Total records:
126
Pages:
1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21
[ 2015 ]
Hofrichter M, Kellner H, Pecyna MJ, Ullrich R Fungal unspecific peroxygenases: heme-thiolate proteins that combine peroxidase and cytochrome p450 properties
Adv. Exp. Med. Biol., 851: 341-368
[ 2015 ]
Kracher D, Zahma K, Schulz C, Sygmund C, Gorton L, Ludwig R Inter-domain electron transfer in cellobiose dehydrogenase: modulation by pH and divalent cations
FEBS J., doi: 10.1111/febs.13310
[ 2015 ]
Linde D, Pogni R, Cañellas M, Lucas F, Guallar V, Baratto MC, Sinicropi A, Saez-Jimenez V, Coscolín C, Romero A, Medrano FJ, Ruiz-Dueñas FJ, Martínez AT Catalytic surface radical in dye-decolorizing peroxidase: A computational, spectroscopic and site-directed mutagenesis study
Biochem. J., 466: 253-262
[ 2015 ]
Linde D, Ruiz-Dueñas FJ, Fernandez-Fueyo E, Guallar V, Hammel KE, Pogni R, Martínez AT Basidiomycete DyPs: Genomic diversity, structural-functional aspects, reaction mechanism and environmental significance
Arch. Biochem. Biophys., 574: 66-74
[ 2015 ]
Maté D, Alcalde M Laccase engineering: From rational design to directed evolution
Biotechnol. Adv., 33: 25-40
[ 2015 ]
Molina-Espeja P, Ma S, Maté D, Ludwig R, Alcalde M Tandem-yeast expression system for engineering and producing unspecific peroxygenase
Enz. Microb. Technol., 73: 29-33
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.
Official webpage of
[ 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