A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass

Autores
Navas, Laura Emilce; Martinez, Fernando; Taverna, María Eugenia; Fetherolf, Morgan M.; Eltis, Lindsay D.; Nicolau, Veronica Viviana; Estenoz, Diana Alejandra; Campos, Eleonora; Benintende, Graciela Beatriz; Berretta, Marcelo Facundo
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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 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.
Instituto de Microbiología y Zoología Agrícola
Fil: Navas, Laura Emilce. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Martinez, Fernando. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina.
Fil: 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; Argentina
Fil: Fetherolf, Morgan M. University of British Columbia. Department of Microbiology & Immunology; Canadá
Fil: Eltis, Lindsay D. University of British Columbia. Department of Microbiology & Immunology; Canadá
Fil: Nicolau, Veronica Viviana. Universidad Tecnológica Nacional. Facultad Regional San Francisco; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: 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; Argentina
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Benintende, Graciela Beatriz. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fuente
AMB Express 9 : 24 (February 2019)
Materia
Lacasa
Oxidorreductasas
Eucalyptus
Biomasa
Delignificación
Potencial Redox
Laccase
Oxidoreductases
Biomass
Delignification
Redox Potential
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/4634
Acceder
id INTADig_c8cca2444d0c84c71114582b515a205c
oai_identifier_str oai:localhost:20.500.12123/4634
network_acronym_str INTADig
repository_id_str l
network_name_str INTA Digital (INTA)
spelling A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomassNavas, Laura EmilceMartinez, FernandoTaverna, María EugeniaFetherolf, Morgan M.Eltis, Lindsay D.Nicolau, Veronica VivianaEstenoz, Diana AlejandraCampos, EleonoraBenintende, Graciela BeatrizBerretta, Marcelo FacundoLacasaOxidorreductasasEucalyptusBiomasaDelignificaciónPotencial RedoxLaccaseOxidoreductasesBiomassDelignificationRedox PotentialLaccases 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.Instituto de Microbiología y Zoología AgrícolaFil: Navas, Laura Emilce. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Martinez, Fernando. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina.Fil: 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; ArgentinaFil: Fetherolf, Morgan M. University of British Columbia. Department of Microbiology & Immunology; CanadáFil: Eltis, Lindsay D. University of British Columbia. Department of Microbiology & Immunology; CanadáFil: Nicolau, Veronica Viviana. Universidad Tecnológica Nacional. Facultad Regional San Francisco; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: 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; ArgentinaFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Benintende, Graciela Beatriz. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; ArgentinaFil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaSpringerOpen2019-03-18T13:36:06Z2019-03-18T13:36:06Z2019-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://amb-express.springeropen.com/articles/10.1186/s13568-019-0748-yhttp://hdl.handle.net/20.500.12123/46342191-0855https://doi.org/10.1186/s13568-019-0748-yAMB Express 9 : 24 (February 2019)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2025-10-16T09:29:28Zoai:localhost:20.500.12123/4634instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-10-16 09:29:28.696INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass
title A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass
spellingShingle A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass
Navas, Laura Emilce
Lacasa
Oxidorreductasas
Eucalyptus
Biomasa
Delignificación
Potencial Redox
Laccase
Oxidoreductases
Biomass
Delignification
Redox Potential
title_short A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass
title_full A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass
title_fullStr A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass
title_full_unstemmed A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass
title_sort A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass
dc.creator.none.fl_str_mv Navas, Laura Emilce
Martinez, Fernando
Taverna, María Eugenia
Fetherolf, Morgan M.
Eltis, Lindsay D.
Nicolau, Veronica Viviana
Estenoz, Diana Alejandra
Campos, Eleonora
Benintende, Graciela Beatriz
Berretta, Marcelo Facundo
author Navas, Laura Emilce
author_facet Navas, Laura Emilce
Martinez, Fernando
Taverna, María Eugenia
Fetherolf, Morgan M.
Eltis, Lindsay D.
Nicolau, Veronica Viviana
Estenoz, Diana Alejandra
Campos, Eleonora
Benintende, Graciela Beatriz
Berretta, Marcelo Facundo
author_role author
author2 Martinez, Fernando
Taverna, María Eugenia
Fetherolf, Morgan M.
Eltis, Lindsay D.
Nicolau, Veronica Viviana
Estenoz, Diana Alejandra
Campos, Eleonora
Benintende, Graciela Beatriz
Berretta, Marcelo Facundo
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Lacasa
Oxidorreductasas
Eucalyptus
Biomasa
Delignificación
Potencial Redox
Laccase
Oxidoreductases
Biomass
Delignification
Redox Potential
topic Lacasa
Oxidorreductasas
Eucalyptus
Biomasa
Delignificación
Potencial Redox
Laccase
Oxidoreductases
Biomass
Delignification
Redox Potential
dc.description.none.fl_txt_mv 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 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.
Instituto de Microbiología y Zoología Agrícola
Fil: Navas, Laura Emilce. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Martinez, Fernando. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina.
Fil: 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; Argentina
Fil: Fetherolf, Morgan M. University of British Columbia. Department of Microbiology & Immunology; Canadá
Fil: Eltis, Lindsay D. University of British Columbia. Department of Microbiology & Immunology; Canadá
Fil: Nicolau, Veronica Viviana. Universidad Tecnológica Nacional. Facultad Regional San Francisco; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: 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; Argentina
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Benintende, Graciela Beatriz. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description 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 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.
publishDate 2019
dc.date.none.fl_str_mv 2019-03-18T13:36:06Z
2019-03-18T13:36:06Z
2019-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://amb-express.springeropen.com/articles/10.1186/s13568-019-0748-y
http://hdl.handle.net/20.500.12123/4634
2191-0855
https://doi.org/10.1186/s13568-019-0748-y
url https://amb-express.springeropen.com/articles/10.1186/s13568-019-0748-y
http://hdl.handle.net/20.500.12123/4634
https://doi.org/10.1186/s13568-019-0748-y
identifier_str_mv 2191-0855
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv SpringerOpen
publisher.none.fl_str_mv SpringerOpen
dc.source.none.fl_str_mv AMB Express 9 : 24 (February 2019)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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