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
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Total records: 112
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[ 2017 ] Acebes S, Ruiz-Dueñas FJ, Toubes M, Saez-Jimenez V, Pérez-Boada M, Lucas F, Martínez AT, Guallar V Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases J. Phys. Chem. B, 121: 3946-3954
[ 2017 ] Alcalde M When directed evolution met ancestral enzyme resurrection Microbial Biotechnol., 10: 22-24
[ 2017 ] Ayuso-Fernández I, Martínez AT, Ruiz-Dueñas FJ Experimental recreation of the evolution of lignin-degrading enzymes from the Jurassic to date Biotechnol. Biofuels, 10: 67
[ 2017 ] Carro J, Martínez A, Medina M, Martínez AT, Ferreira P Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase Phys. Chem. Chem. Phys., doi: 10.1039/C7CP05904C
[ 2017 ] González-Pérez D, Alcalde M The making of versatile peroxidase by directed evolution Biocatalysis and Biotransformation, doi: 10.1080/10242422.2017.1363190
[ 2017 ] Martínez AT, Ruiz-Dueñas FJ, Camarero S, Serrano A, Linde D, Lund H, Vind J, Tovborg M, Herold-Majumdar OM, Hofrichter M, Liers C, Ullrich R, Scheibner K, Sannia G, Piscitelli A, Sener ME, Kılıç S, van Berkel WJ, Guallar V, et al. Oxidoreductases on their way to industrial biotransformations Biotechnol. Adv., doi: 10.1016/j.biotechadv.2017.06.003
Experimental recreation of the evolution of lignin-degrading enzymes from the Jurassic to date
Ayuso-Fernández I, Martínez AT, Ruiz-Dueñas FJ
Biotechnol. Biofuels, 10: 67


Floudas et al. (Science 336: 1715) established that lignin-degrading fungi appeared at the end of Carboniferous period associated with the production of the first ligninolytic peroxidases. Here, the subsequent evolution of these enzymes in Polyporales, where most wood-rotting fungi are included, is experimentally recreated using genomic information.


With this purpose, we analyzed the evolutionary pathway leading to the most efficient lignin-degrading peroxidases characterizing Polyporales species. After sequence reconstruction from 113 genes of ten sequenced genomes, the main enzyme intermediates were resurrected and characterized. Biochemical changes were analyzed together with predicted sequences and structures, to understand how these enzymes acquired the ability to degrade lignin and how this ability changed with time. The most probable first peroxidase in Polyporales would be a manganese peroxidase (Mn3+ oxidizing phenolic lignin) that did not change substantially until the appearance of an exposed tryptophan (oxidizing nonphenolic lignin) originating an ancestral versatile peroxidase. Later, a quick evolution, with loss of the Mn2+-binding site, generated the first lignin peroxidase that evolved to the extant form by improving the catalytic efficiency. Increased stability at acidic pH, which strongly increases the oxidizing power of these enzymes, was observed paralleling the appearance of the exposed catalytic tryptophan.


We show how the change in peroxidase catalytic activities meant an evolutionary exploration for more efficient ways of lignin degradation by fungi, a key step for carbon recycling in land ecosystems. The study provides ancestral enzymes with a potential biotechnological interest for the sustainable production of fuels and chemicals in a biomass-based economy.

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