Optimized oxidoreductases for medium and large scale industrial biotransformations
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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
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publications
Total records: 124
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[ 2014 ] Rico A, Rencoret J, del Río JC, Martínez AT, Gutiérrez A Pretreatment with laccase and a phenolic mediator degrades lignin and enhances saccharification of Eucalyptus feedstock Biotechnol. Biofuels, 7: 6
[ 2013 ] Babot ED, del Río JC, Kalum L, Martínez AT, Gutiérrez A Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from Coprinopsis cinerea Biotechnol. Bioeng., 110: 2323-2332
[ 2013 ] Bey M, Zhou S, Poidevin L, Henrissat B, Coutinho PM, Berrin JG, Sigoillot JC Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina Appl. Environ. Microbiol., 79: 488-496
[ 2013 ] Carabajal M, Kellner H, Levin L, Jehmlich N, Hofrichter M, Ullrich R The secretome of Trametes versicolor grown on tomato juice medium and purification of the secreted oxidoreductases including a versatile peroxidase J. Biotech., 168: 15-23
[ 2013 ] Churakova E, Arends IWCE, Hollmann F Increasing the Productivity of Peroxidase-Catalyzed Oxyfunctionalization: A Case Study on the Potential of Two-Liquid-Phase Systems ChemCatChem, 5: 565-568
[ 2013 ] Hahn F, Ullrich R, Hofrichter M, Liers C Experimental approach to follow the spatiotemporal wood degradation in fungal microcosms Biotechnol. J., 8: 127-132
year2019
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