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
[ 2019 ]
Linde D, Ayuso-Fernández I, Ruiz-Dueñas FJ, Martínez AT Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan
Arch. Biochem. Biophys., 668: 23-28
[ 2019 ]
Serrano A, Sancho F, Viña-Gonzalez J, Carro J, Alcalde M, Guallar V, Martínez AT Switching the substrate preference of fungal aryl-alcohol oxidase: towards stereoselective oxidation of secondary benzyl alcohols
Catal. Sci. Technol., doi: 10.1039/C8CY02447B
[ 2019 ]
Viña-Gonzalez J, Jimenez-Lalana D, Sancho F, Serrano A, Martínez AT, Guallar V, Alcalde M Structure‐Guided Evolution of Aryl Alcohol Oxidase from Pleurotus eryngii for the Selective Oxidation of Secondary Benzyl Alcohols
Adv. Synth. Catal., 361: 2514-2525
[ 2018 ]
Carro J, Fernandez-Fueyo E, Fernández-Alonso C, Cañada J, Ullrich R, Hofrichter M, Alcalde M, Ferreira P, Martínez AT Self-sustained enzymatic cascade for the production of 2,5-furandicarboxylic acid from 5-methoxymethylfurfural
Biotechnol. Biofuels, 11: 86-96
[ 2018 ]
Carro J, Ferreira P, Martínez AT, Gadda G Stepwise Hydrogen Atom and Proton Transfers in Dioxygen Reduction by Aryl-Alcohol Oxidase
Biochemistry, doi: 10.1021/acs.biochem.8b00106
[ 2018 ]
Ewing TA, Kühn J, Segarra S, Tortajada M, Zuhse R, van Berkel WJ Multigram Scale Enzymatic Synthesis of (R)‐1‐(4′‐Hydroxyphenyl)ethanol Using Vanillyl Alcohol Oxidase
Adv. Synth. Catal., 360: 2370-2376
year2016
Extracellular electron transfer systems fuel cellulose oxidative degradation
Kracher D, Scheiblbrandner S, Felice AKG, Breslmayr E, Preims M, Ludwicka K, Haltrich D, Eijsink VG, Ludwig R
Science, 352: 1098-1101
Ninety percent of lignocellulose-degrading fungi contain genes encoding lytic polysaccharide monooxygenases (LPMOs). These enzymes catalyze the initial oxidative cleavage of recalcitrant polysaccharides after activation by an electron donor. Understanding the source of electrons is fundamental to fungal physiology and will also help exploit LPMOs for biomass processing. Using genome data and biochemical methods, we characterized and compared different extracellular electron sources for LPMO: cellobiose dehydrogenase, phenols procured from plant biomass or produced by fungi, and GMC oxidoreductases that regenerate LPMO-reducing diphenols. These data demonstrate that all three electron transfer systems are functional and that their relative importance during cellulose degradation depends on fungal lifestyle. The availability of extracellular electron donors is obligatory to activate fungal oxidative attack on polysaccharides.
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