Optimized oxidoreductases for medium and large scale industrial biotransformations
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Dr Marta Pérez-Boada
E-mail: MPBoada@cib.csic.es
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publications
Total records: 126
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[ 2016 ] van Kuijk SJA, del Río JC, Rencoret J, Gutiérrez A, Sonnenberg ASM, Baars JJP, Hendriks WH, Cone JW Selective ligninolysis of wheat straw and wood chips by the white-rot fungus Lentinula edodes and its influence on in vitro rumen degradability J. Anim. Sci. Biotechnol., 7: 55
[ 2016 ] Viña-Gonzalez J, González-Pérez D, Alcalde M Directed evolution method in Saccharomyces cerevisiae: Mutant library creation and screening J. Vis. Exp., doi: 10.3791/53761
[ 2015 ] Alcalde M Engineering the ligninolytic enzyme consortium Trends Biotechnol., 33: 155-162
[ 2015 ] Babot ED, del Río JC, Cañellas M, Sancho F, Lucas F, Guallar V, Kalum L, Lund H, Gröbe G, Scheibner K, Ullrich R, Hofrichter M, Martínez AT, Gutiérrez A Steroid hydroxylation by basidiomycete peroxygenases: A combined experimental and computational study Appl. Environ. Microbiol., doi: 10.1128/AEM.00660-15
[ 2015 ] Babot ED, del Río JC, Kalum L, Martínez AT, Gutiérrez A Regioselective Hydroxylation in the Production of 25-Hydroxyvitamin D by Coprinopsis cinerea Peroxygenase ChemCatChem, 7: 283-290
[ 2015 ] Baratto MC, Sinicropi A, Linde D, Saez-Jimenez V, Sorace L, Ruiz-Dueñas FJ, Martínez AT, Basosi R, Pogni R Redox-Active Sites in Auricularia auricula-judae Dye-Decolorizing Peroxidase and Several Directed Variants: A Multifrequency EPR Study J. Phys. Chem. B, 119: 13583-13592
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.

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