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
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[ 2014 ] Barrasa JM, Blanco MN, Esteve-Raventós F, Altés A, Checa J, Martínez AT, Ruiz-Dueñas FJ Wood and humus decay strategies by white-rot basidiomycetes correlate with two different dye decolorization and enzyme secretion patterns on agar plates Fungal Gen. Biol., doi: 10.1016/j.fgb.2014.03.007
[ 2014 ] Camarero S, Martínez MJ, Martínez AT Understanding lignin biodegradation for the improved utilization of plant biomass in modern biorefineries Biofuels, Bioprod. Bioref., 8: 615-625
[ 2014 ] Carro J, Ferreira P, Rodríguez L, Prieto A, Serrano A, Balcells B, Ardá A, Jiménez-Barbero J, Gutiérrez A, Ullrich R, Hofrichter M, Martínez AT 5-Hydroxymethylfurfural conversion by fungal aryl-alcohol oxidase and unspecific peroxygenase FEBS J., 282: 3218-3229
[ 2014 ] Fernandez-Fueyo E, Acebes S, Ruiz-Dueñas FJ, Martínez MJ, Romero A, Medrano FJ, Guallar V, Martínez AT Structural implications of the C-terminal tail in the catalytic and stability properties of manganese peroxidases from ligninolytic fungi Acta Crystal. D, 70: 3253-3265
[ 2014 ] Fernandez-Fueyo E, Castanera ER, Ruiz-Dueñas FJ, López-Lucendo MF, Ramírez L, Pisabarro AG, Martínez AT Ligninolytic peroxidase gene expression by Pleurotus ostreatus: Differential regulation in lignocellulose medium and effect of temperature and pH Fungal Gen. Biol., doi: 10.1016/j.fgb.2014.02.003
[ 2014 ] Fernandez-Fueyo E, Ruiz-Dueñas FJ, Martínez AT Engineering a fungal peroxidase that degrades lignin at very acidic pH Biotechnol. Biofuels, 7: 114
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