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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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Autores principales: Navas, Laura E., Martínez, Fernando D., Taverna, María E., Fetherolf, Morgan M., Eltis, Lindsay D., Nicolau, Verónica, Estenoz, Diana, Campos, Eleonora, Benintende, Graciela B., Berretta, Marcelo F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6372703/
https://www.ncbi.nlm.nih.gov/pubmed/30756202
http://dx.doi.org/10.1186/s13568-019-0748-y
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author Navas, Laura E.
Martínez, Fernando D.
Taverna, María E.
Fetherolf, Morgan M.
Eltis, Lindsay D.
Nicolau, Verónica
Estenoz, Diana
Campos, Eleonora
Benintende, Graciela B.
Berretta, Marcelo F.
author_facet Navas, Laura E.
Martínez, Fernando D.
Taverna, María E.
Fetherolf, Morgan M.
Eltis, Lindsay D.
Nicolau, Verónica
Estenoz, Diana
Campos, Eleonora
Benintende, Graciela B.
Berretta, Marcelo F.
author_sort Navas, Laura E.
collection PubMed
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 (k(cat)/K(M)) 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13568-019-0748-y) contains supplementary material, which is available to authorized users.
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spelling pubmed-63727032019-03-04 A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass Navas, Laura E. Martínez, Fernando D. Taverna, María E. Fetherolf, Morgan M. Eltis, Lindsay D. Nicolau, Verónica Estenoz, Diana Campos, Eleonora Benintende, Graciela B. Berretta, Marcelo F. AMB Express Original Article 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 (k(cat)/K(M)) 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13568-019-0748-y) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2019-02-12 /pmc/articles/PMC6372703/ /pubmed/30756202 http://dx.doi.org/10.1186/s13568-019-0748-y Text en © The Author(s) 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Original Article
Navas, Laura E.
Martínez, Fernando D.
Taverna, María E.
Fetherolf, Morgan M.
Eltis, Lindsay D.
Nicolau, Verónica
Estenoz, Diana
Campos, Eleonora
Benintende, Graciela B.
Berretta, Marcelo F.
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 Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6372703/
https://www.ncbi.nlm.nih.gov/pubmed/30756202
http://dx.doi.org/10.1186/s13568-019-0748-y
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