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

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 The...

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Main Authors: 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
Format: Artículo
Language:Inglés
Published: SpringerOpen 2019
Subjects:
Online Access: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
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author 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_browse Benintende, Graciela Beatriz
Berretta, Marcelo Facundo
Campos, Eleonora
Eltis, Lindsay D.
Estenoz, Diana Alejandra
Fetherolf, Morgan M.
Martinez, Fernando
Navas, Laura Emilce
Nicolau, Veronica Viviana
Taverna, María Eugenia
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_sort Navas, Laura Emilce
collection INTA Digital
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.
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spelling INTA46342020-01-07T15:40:48Z A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass 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 Lacasa Oxidorreductasas Eucalyptus Biomasa Delignificación Potencial Redox Laccase Oxidoreductases Biomass Delignification Redox Potential 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 2019-03-18T13:36:06Z 2019-03-18T13:36:06Z 2019-02 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 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 eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf SpringerOpen AMB Express 9 : 24 (February 2019)
spellingShingle Lacasa
Oxidorreductasas
Eucalyptus
Biomasa
Delignificación
Potencial Redox
Laccase
Oxidoreductases
Biomass
Delignification
Redox Potential
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
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
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_short A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass
title_sort thermostable laccase from thermus sp 2 9 and its potential for delignification of eucalyptus biomass
topic Lacasa
Oxidorreductasas
Eucalyptus
Biomasa
Delignificación
Potencial Redox
Laccase
Oxidoreductases
Biomass
Delignification
Redox Potential
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
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