Optimized oxidoreductases for medium and large scale industrial biotransformations
Total records:
126
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[ 2016 ]
Maté D, Alcalde M Laccase: a multi-purpose biocatalyst at the forefront of biotechnology
Microbial Biotechnol., doi: 10.1111/1751-7915.12422
[ 2016 ]
Mathieu Y, Piumi F, Valli R, Carro J, Ferreira P, Faulds CB, Record E Activities of Secreted Aryl Alcohol Quinone Oxidoreductases from Pycnoporus cinnabarinus Provide Insights into Fungal Degradation of Plant Biomass
Appl. Environ. Microbiol., 82: 2411-2423
[ 2016 ]
Molina-Espeja P, Cañellas M, Plou FJ, Hofrichter M, Lucas F, Guallar V, Alcalde M Synthesis of 1-Naphthol by a Natural Peroxygenase engineered by Directed Evolution
ChemBioChem, 17: 341-349
[ 2016 ]
Molina-Espeja P, Viña-Gonzalez J, Gomez-Fernandez BJ, Martin-Diaz J, García-Ruiz E, Alcalde M Beyond the outer limits of nature by directed evolution
Biotechnol. Adv., 34: 754-767
[ 2016 ]
Ni Y, Fernandez-Fueyo E, Gomez Baraibar A, Ullrich R, Hofrichter M, Yanase H, Alcalde M, van Berkel WJ, Hollmann F Peroxygenase-Catalyzed Oxyfunctionalization Reactions Promoted by the Complete Oxidation of Methanol
Angew. Chem. Int. Ed., 55: 798-801
[ 2016 ]
Olmedo A, Aranda C, del Río JC, Kiebist J, Scheibner K, Martínez AT, Gutiérrez A From Alkanes to Carboxylic Acids: Terminal Oxygenation by a Fungal Peroxygenase
Angew. Chem. Int. Ed., 55: 12248-12251
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.
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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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