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Abstract
Laccases 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 [ver mas...]
dc.contributor.authorNavas, Laura Emilce
dc.contributor.authorMartinez, Fernando
dc.contributor.authorTaverna, María Eugenia
dc.contributor.authorFetherolf, Morgan M.
dc.contributor.authorEltis, Lindsay D.
dc.contributor.authorNicolau, Veronica Viviana
dc.contributor.authorEstenoz, Diana Alejandra
dc.contributor.authorCampos, Eleonora
dc.contributor.authorBenintende, Graciela Beatriz
dc.contributor.authorBerretta, Marcelo Facundo
dc.date.accessioned2019-03-18T13:36:06Z
dc.date.available2019-03-18T13:36:06Z
dc.date.issued2019-02
dc.identifier.issn2191-0855
dc.identifier.otherhttps://doi.org/10.1186/s13568-019-0748-y
dc.identifier.urihttps://amb-express.springeropen.com/articles/10.1186/s13568-019-0748-y
dc.identifier.urihttp://hdl.handle.net/20.500.12123/4634
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.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherSpringerOpenes_AR
dc.rightsinfo:eu-repo/semantics/openAccesses_AR
dc.sourceAMB Express 9 : 24 (February 2019)es_AR
dc.subjectLacasaes_AR
dc.subjectLaccaseeng
dc.subjectOxidorreductasases_AR
dc.subjectOxidoreductaseseng
dc.subjectEucalyptuses_AR
dc.subjectBiomasaes_AR
dc.subjectBiomasseng
dc.subjectDelignificaciónes_AR
dc.subjectDelignificationeng
dc.subjectPotencial Redoxes_AR
dc.subjectRedox Potentialeng
dc.titleA thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomasses_AR
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articlees_AR
dc.typeinfo:eu-repo/semantics/publishedVersiones_AR
dc.description.origenInstituto de Microbiología y Zoología Agrícolaes_AR
dc.description.filFil: Navas, Laura Emilce. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Martinez, Fernando. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina.es_AR
dc.description.filFil: Taverna, María Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina. Universidad Tecnológica Nacional. Facultad Regional San Francisco; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Fetherolf, Morgan M. University of British Columbia. Department of Microbiology & Immunology; Canadáes_AR
dc.description.filFil: Eltis, Lindsay D. University of British Columbia. Department of Microbiology & Immunology; Canadáes_AR
dc.description.filFil: Nicolau, Veronica Viviana. Universidad Tecnológica Nacional. Facultad Regional San Francisco; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Estenoz, Diana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina.Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Benintende, Graciela Beatriz. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentinaes_AR
dc.description.filFil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.subtypecientifico


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