Optimized oxidoreductases for medium and large scale industrial biotransformations
Project Secretariat
Dr Marta Pérez-Boada
E-mail: MPBoada@cib.csic.es
Consejo Superior de Investigaciones Científicas (CSIC)
Biological Research Centre (CIB)
Calle Ramiro de Maeztu 9, E-28040 Madrid, Spain
Phone: 34 918373112
Fax: 34 915360432
Mobile: 34 650080476
Private area


Total records: 124
Pages:    1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21  

[ 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
[ 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
Switching the substrate preference of fungal aryl-alcohol oxidase: towards stereoselective oxidation of secondary benzyl alcohols
Serrano A, Sancho F, Viña-Gonzalez J, Carro J, Alcalde M, Guallar V, Martínez AT
Catal. Sci. Technol., doi: 10.1039/C8CY02447B

Oxidation of primary alcohols by aryl-alcohol oxidase (AAO), a flavoenzyme that provides H2O2 to fungal peroxidases for lignin degradation in nature, is achieved by concerted hydroxyl proton transfer and stereoselective hydride abstraction from the pro-R benzylic position. In racemic secondary alcohols, the R-hydrogen abstraction would result in the selective oxidation of the S-enantiomer to the corresponding ketone. This stereoselectivity of AAO may be exploited for enzymatic deracemization of chiral mixtures and isolation of R-enantiomers of industrial interest by switching the enzyme activity from primary to secondary alcohols. A combination of computational simulations and mutagenesis has been used to produce AAO variants with increased activity on secondary alcohols, using the already available F501A variant of Pleurotus eryngii AAO as a starting point. Adaptive-PELE simulations for the diffusion of (S)-1-(p-methoxyphenyl)-ethanol in this variant allowed Ile500 to be identified as one of the key residues with a higher number of contacts with the substrate during its transition from the solvent to the active site. Substitution of Ile500 produced more efficient variants for the oxidation of several secondary alcohols, and the I500M/F501W double variant was able to fully oxidize (after 75 min) with high selectivity (ee >99%) the S-enantiomer of the model secondary aryl-alcohol (±)-1-(p-methoxyphenyl)-ethanol, while the R-enantiomer remained unreacted.

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