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)
Calle Ramiro de Maeztu 9, E-28040 Madrid, Spain
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publications
Total records: 126
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[ 2015 ] Viña-Gonzalez J, González-Pérez D, Ferreira P, Martínez AT, Alcalde M Focused directed evolution of aryl-alcohol oxidase in yeast using chimeric signal peptides Appl. Environ. Microbiol., 81: 6451-6462
[ 2015 ] Wang X, Ullrich R, Hofrichter M, Groves JT Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive Proc. Natl. Acad. Sci. USA, 112: 3686-3691
[ 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
year2014
A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides
Isaksen T, Westereng B, Aachmann FL, Agger JW, Kracher D, Kittl R, Ludwig R, Haltrich D, Eijsink VG, Horn SJ
J. Biol. Chem., 289: 2632-2642

Lignocellulosic biomass is a renewable resource that significantly can substitute fossil resources for the production of fuels, chemicals, and materials. Efficient saccharification of this biomass to fermentable sugars will be a key technology in future biorefineries. Traditionally, saccharification was thought to be accomplished by mixtures of hydrolytic enzymes. However, recently it has been shown that lytic polysaccharide monooxygenases (LPMOs) contribute to this process by catalyzing oxidative cleavage of insoluble polysaccharides utilizing a mechanism involving molecular oxygen and an electron donor. These enzymes thus represent novel tools for the saccharification of plant biomass. Most characterized LPMOs, including all reported bacterial LPMOs, form aldonic acids, i.e., products oxidized in the C1 position of the terminal sugar. Oxidation at other positions has been observed, and there has been some debate concerning the nature of this position (C4 or C6). In this study, we have characterized an LPMO from Neurospora crassa (NcLPMO9C; also known as NCU02916 and NcGH61-3). Remarkably, and in contrast to all previously characterized LPMOs, which are active only on polysaccharides, NcLPMO9C is able to cleave soluble cello-oligosaccharides as short as a tetramer, a property that allowed detailed product analysis. Using mass spectrometry and NMR, we show that the cello-oligosaccharide products released by this enzyme contain a C4 gemdiol/keto group at the nonreducing end.

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