Optimized oxidoreductases for medium and large scale industrial biotransformations
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Dr Marta Pérez-Boada
E-mail: MPBoada@cib.csic.es
Consejo Superior de Investigaciones Científicas (CSIC)
Biological Research Centre (CIB)
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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
Oxidation and nitration of mononitrophenols by a DyP-type peroxidase
Büttner E, Ullrich R, Strittmatter E, Piontek K, Plattner D, Hofrichter M, Liers C
Arch. Biochem. Biophys., 574: 86-92

Substantial conversion of nitrophenols, typical high-redox potential phenolic substrates, by heme peroxidases has only been reported for lignin peroxidase (LiP) so far. But also a dye-decolorizing peroxidase of Auricularia auricula-judae (AauDyP) was found to be capable of acting on (i) ortho-nitrophenol (oNP), (ii) meta-nitrophenol (mNP) and (iii) para-nitrophenol (pNP). The pH dependency for pNP oxidation showed an optimum at pH 4.5, which is typical for phenol conversion by DyPs and other heme peroxidases. In the case of oNP and pNP conversion, dinitrophenols (2,4-DNP and 2,6-DNP) were identified as products and for pNP additionally p-benzoquinone. Moreover, indications were found for the formation of random polymerization products originating from initially formed phenoxy radical intermediates. Nitration was examined using 15N-labeled pNP and Na14NO2 as an additional source of nitro-groups. Products were identified by HPLC–MS, and mass-to-charge ratios were evaluated to clarify the origin of nitro-groups. The additional nitrogen in DNPs formed during enzymatic conversion was found to originate both from 15N-pNP and 14NO2Na. Based on these results, a hypothetical reaction scheme and a catalytically responsible confine of the enzyme’s active site are postulated.

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