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dc.coverage.spatialInternacionales_ES
dc.creatorNavas, Laura
dc.creatorMartinez, Fernando
dc.creatorTaverna, María Eugenia
dc.creatorFetherol, Morgan
dc.creatorEltis, Lindsay
dc.creatorNicolau, Verónica V.
dc.creatorEstenoz, Diana
dc.creatorCampos, Eleonora
dc.creatorBenintende, Graciela
dc.creatorBerreta, Marcelo
dc.date.accessioned2019-02-26T21:02:55Z
dc.date.available2019-02-26T21:02:55Z
dc.date.issued2019-04-02
dc.identifier.citationNavas, Laura; Martinez, Fernando; Taverna, María Eugenia; Fetherol, Morgan; Eltis, Lindsay; Nicolau, Verónica; Estenoz, Diana; Campos, Eleonora; Benintende, Graciela; Berretta, Marcelo; A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass; AMB Express; 2 de abril del 2019.es_ES
dc.identifier.urihttp://hdl.handle.net/123456789/3436
dc.description.abstractLaccases are multicopper oxidases that are being studied for their potential application in pretreatment strategies of lignocellulosic feedstocks for bioethanol production. Here, we report the expression and characterization of a predicted laccase (LAC_2.9) from the thermophilic bacterial strain Thermus sp. 2.9 and investigate its capacity to delignify lignocellulosic biomass. The purified enzyme displayed a blue color typical of laccases, showed strict copper dependence and retained 80% of its activity after 16 h at 70 °C. At 60 °C, the enzyme oxidized 2,2′-azino-di-(3-ethylbenzthiazoline sulfonate) (ABTS) and 2,6-dimethoxyphenol (DMP) at optimal pH of 5 and 6, respectively. LAC_2.9 had higher substrate specificity (kcat/KM) for DMP with a calculated value that accounts for one of the highest reported for laccases. Further, the enzyme oxidized a phenolic lignin model dimer. The incubation of steam-exploded eucalyptus biomass with LAC_2.9 and 1-hydroxybenzotriazole (HBT) as mediator changed the structural properties of the lignocellulose as evidenced by Fourier transform infrared (FTIR) spectroscopy and thermo-gravimetric analysis (TGA). However, this did not increase the yield of sugars released by enzymatic saccharification. In conclusion, LAC_2.9 is a thermostable laccase with potential application in the delignification of lignocellulosic biomass.es_ES
dc.formatapplication/pdfes_ES
dc.language.isoenges_ES
dc.language.isoenges_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.rights.uriAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.rights.uriAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.subjectdelignificationes_ES
dc.subjectEucalyptus globulus biomasses_ES
dc.subjectredox mediatores_ES
dc.subjectthermostable bacterial laccasees_ES
dc.subjectthermuses_ES
dc.titleA thermostable laccase from Thermus sp. 2.9 and its potential for delignifcation of Eucalyptus biomasses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.description.affiliationNavas, Laura(1); Martinez, Fernando (1); Taverna, María Eugenia (2,3); Fetherol, Morgan (4,5); Nicolau, Verónica (2); Estenoz, Diana (3); Campos, Eleonora (1);Berretta, Marcelo (1) (1) Instituto de Microbiología y Zoología Agrícola, Instituto Nacional de Tecnología Agropecuaria (INTA), Nicolás Repetto y De los Reseros s/n., 1686 Hurlingham, Buenos Aires, Argentina. . (2) UTN Regional San Francisco, Av. de la Universidad 501, (2400) San Francisco, Córdoba, Argentina; (3) INTEC (UNL-CONICET), Güemes 3450, (3000) Santa Fe, Argentina. (4) Department of Microbiology & Immunology, The University of British Columbia, Vancouver, BC V6T 1Z3, Canada. Eltis, Lindsay. Department of Microbiology & Immunology, The University of British Columbia, Vancouver, BC V6T 1Z3, Canada. (5) Instituto de Biotecnología, Instituto Nacional de Tecnología.es_ES
dc.description.peerreviewedPeer Reviewedes_ES
dc.type.versioninfo:eu-repo/semantics/publisherVersiones_ES
dc.type.snrdinfo:ar-repo/semantics/artículoes_ES
dc.identifier.doihttp://10.1186/s13568-019-0748-y


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