Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2016 ]
Pardo I, Santiago G, Gentili P, Lucas F, Monza E, Medrano FJ, Galli C, Martínez AT, Guallar V, Camarero S Re-designing the substrate binding pocket of laccase for enhanced oxidation of sinapic acid
Catal. Sci. Technol., doi: 10.1039/C5CY01725D
[ 2016 ]
Rencoret J, Pereira A, del Río JC, Martínez AT, Gutiérrez A Laccase-Mediator Pretreatment of Wheat Straw Degrades Lignin and Improves Saccharification
Bioenerg. Res., 9: 917-930
[ 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
year2015
Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II)
Fernandez-Fueyo E, Linde D, Almendral D, López-Lucendo MF, Ruiz-Dueñas FJ, Martínez AT
Appl. Microbiol. Biotechnol., doi: 10.1007/s00253-015-6665-3
Two phylogenetically divergent genes of the new family of dye-decolorizing peroxidases (DyPs) were found during comparison of the four DyP genes identified in the Pleurotus ostreatus genome with over 200 DyP genes from other basidiomycete genomes. The heterologously expressed enzymes (Pleos-DyP1 and Pleos-DyP4, following the genome nomenclature) efficiently oxidize anthraquinoid dyes (such as Reactive Blue 19), which are characteristic DyP substrates, as well as low redox-potential dyes (such as 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)) and substituted phenols. However, only Pleos-DyP4 oxidizes the high redox-potential dye Reactive Black 5, at the same time that it displays high thermal and pH stability. Unexpectedly, both enzymes also oxidize Mn2+ to Mn3+, albeit with very different catalytic efficiencies. Pleos-DyP4 presents a Mn2+ turnover (56 s-1) nearly in the same order of the two other Mn2+-oxidizing peroxidase families identified in the P. ostreatus genome: manganese peroxidases (100 s-1 average turnover) and versatile peroxidases (145 s-1 average turnover), whose genes were also heterologously expressed. Oxidation of Mn2+ has been reported for an Amycolatopsis DyP (24 s-1) and claimed for other bacterial DyPs, albeit with lower activities, but this is the first time that Mn2+ oxidation is reported for a fungal DyP. Interestingly, Pleos-DyP4 (together with ligninolytic peroxidases) is detected in the secretome of P. ostreatus grown on different lignocellulosic substrates. It is suggested that generation of Mn3+ oxidizers plays a role in the P. ostreatus white-rot lifestyle since three different families of Mn2+-oxidizing peroxidase genes are present in its genome being expressed during lignocellulose degradation. Open Access
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[ 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
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