Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/159764

COMPARTIR / EXPORTAR:

SHARE BASE	Comparte tu historia de Acceso Abierto
Visualizar otros formatos: MARC \| Dublin Core \| RDF \| ORE \| MODS \| METS \| DIDL \| DATACITE
Refman EndNote Bibtex RefWorks Excel CSV PDF DataCite Send via email

Título:	Oxidoreductases of industrial interest: the INDOX EU-Project
Autor:	Ruiz-Dueñas, F. J. CSIC ORCID ; Camarero, Susana CSIC ORCID ; Gutiérrez Suárez, Ana CSIC ORCID ; Río Andrade, José Carlos del CSIC ORCID ; Alcalde Galeote, Miguel CSIC ORCID ; Pérez-Boada, Marta CSIC ORCID ; Martínez, Ángel T. CSIC ORCID
Fecha de publicación:	3-jul-2016
Editor:	Wageningen Academic Publishers
Citación:	OxiZymes 2016 (8th European Meeting on OxiZymes) 3–6 July 2016 (Wageningen) Netherlands
Resumen:	the INDOX project (www.Indoxproject.eu) aims to provide relevant industrial case stories lo Demonstrate the efficiency of optimized oxidoreductase biocatalysts on targeted reactions, including intermediates for agrochemicals, APIs and dye-stuffs, as well as polymer precursors and functionalized polymers. The project flow comprises: (1) recovery of selective biocatalysts from fungal genomes and other sources; (2) improvement of their activity and stability by protein engineering to fulfil the operational and catalytic conditions required by the chemical industry; and (3) optimization of reaction conditions. Finally, the cost efficiency is evaluated. A diversity of genes were identified from genomes coding: (1) heme-peroxidases (heme-thiolate peroxygenases, dye-decolorizing perroxidases and classical peroxidases); (2) flavor-oxidases (vanillyl- alcohol and aryl-alcohol oxidases and cellobiose dehydrogenases); and (3) Cu-oxidoreductases (laccases and lytic polysaccharide monooxygenases). The most promising candidates were expressed in laboratory (and industrial) hosts and biochemically/structurally characterized. Rational enzyme engineering assisted by computational prediction was used to obtain binding, oxidative stability and operational improvements, while laboratory directed evolution allowed their adaptation to bioprocess requirements and the generation of more thermostable and alkalophilic enzymes. For developing industrially feasible bioprocesses, several parameters are being analyzed and optimized, including enzyme immobilization, two-liquid phase system, solvent free reactions and in situ peroxide generation, as well as bienzymatic cascade reaction using peroxygenases and oxidases. The above optimized enzymes and bioprocess are being applied for; (1) oxyfunctionalization reactions (of aliphatic and aromatic compounds) resulting in hydroxyl, epoxy, oxo and carboxy derivatives with different region- and stereo-selectivities; and (2) oxidation reactions, including coupling of phenols and other aromatics for polymers and dyes, production of chemical building blocks, cross-linking of feruloyl-arabinoxylans, and oxidative modification of aromatic compounds and lignin
Descripción:	Póster presentado en OxiZymes 2016 (8th European Meeting on OxiZymes) 3–6 July 2016 (Wageningen) Netherlands.-- Ruiz-Dueñas, F. J. et al... [ ]
URI:	http://hdl.handle.net/10261/159764
Aparece en las colecciones:	(IRNAS) Comunicaciones congresos (CIB) Comunicaciones congresos (ICP) Comunicaciones congresos