Optimized oxidoreductases for medium and large scale industrial biotransformations
Total records:
126
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[ 2016 ]
Pardo I, Santiago G, Gentili P, Lucas F, Monza E, Medrano FJ, Galli C, Martínez AT, Guallar V, Camarero S Re-designing the substrate binding pocket of laccase for enhanced oxidation of sinapic acid
Catal. Sci. Technol., doi: 10.1039/C5CY01725D
[ 2016 ]
Rencoret J, Pereira A, del Río JC, Martínez AT, Gutiérrez A Laccase-Mediator Pretreatment of Wheat Straw Degrades Lignin and Improves Saccharification
Bioenerg. Res., 9: 917-930
[ 2016 ]
Saez-Jimenez V, Acebes S, García-Ruiz E, Romero A, Guallar V, Alcalde M, Medrano FJ, Martínez AT, Ruiz-Dueñas FJ Unveiling the basis of alkaline stability of an evolved versatile peroxidase
Biochem. J., 473: 1917-1928
[ 2016 ]
Saez-Jimenez V, Rencoret J, Rodríguez-Carvajal MA, Gutiérrez A, Ruiz-Dueñas FJ, Martínez AT Role of surface tryptophan for peroxidase oxidation of nonphenolic lignin
Biotechnol. Biofuels, 9: 198-211
[ 2016 ]
Salvachúa D, Katahira R, Cleveland NS, Khanna P, Resch MG, Black BA, Purvine SO, Zink EM, Prieto A, Martínez MJ, Martínez AT, Simmons BA, Gladden JM, Beckham GT Lignin depolymerization by fungal secretomes and a microbial sink
Green Chem., doi: 10.1039/C6GC01531J
[ 2016 ]
Santiago G, de Salas F, Lucas F, Monza E, Acebes S, Martínez AT, Camarero S, Guallar V Computer-Aided Laccase Engineering: Toward Biological Oxidation of Arylamines
ACS-Catalysis, 6: 5415-5423
year2015
Regioselective Hydroxylation in the Production of 25-Hydroxyvitamin D by Coprinopsis cinerea Peroxygenase
Babot ED, del Río JC, Kalum L, Martínez AT, Gutiérrez A
ChemCatChem, 7: 283-290
Monohydroxylated metabolites of vitamin D3 (cholecalciferol) and vitamin D2 (ergocalciferol), generically known as 25-hydroxycalciferol, are better for several diseases, and other applications, than vitamin D (calciferol). This work describes a novel biotechnological approach for the preparation of 25-hydroxycalciferols, starting from readily available cholecalciferol and ergocalciferol. This approach enables the regioselective (100 %) hydroxylation of these compounds (at the C-25 position) under mild and environmentally friendly conditions by using a peroxidase from the fungus Coprinopsis cinerea (gene model CC1G_08427T0 from the sequenced genome), which catalyzes monooxygenation with H2O2 as the only co-substrate (peroxygenase). Hydroxylation of cholecalciferol and ergocalciferol is a true peroxygenation, as demonstrated by incorporation of 18O from H218O2 into the products. The peroxygenase has additional advantages related to its recombinant nature, enabling enzyme engineering and low-cost overexpression in an industrial host. Therefore, the peroxygenase is a promising biocatalyst for the production of vitamin D active metabolites.
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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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