A thermostable laccase from Thermus sp. 2.9 and its potential for delignifcation 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: | , , , , , , , , , |
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| Formato: | Artículo publishedVersion |
| Lenguaje: | Inglés Inglés |
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2019
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| Acceso en línea: | http://hdl.handle.net/20.500.12272/3436 http://10.1186/s13568-019-0748-y |
| Aporte de: |
| id |
I68-R174-20.500.12272-3436 |
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| record_format |
dspace |
| institution |
Universidad Tecnológica Nacional |
| institution_str |
I-68 |
| repository_str |
R-174 |
| collection |
RIA - Repositorio Institucional Abierto (UTN) |
| language |
Inglés Inglés |
| topic |
delignification Eucalyptus globulus biomass redox mediator thermostable bacterial laccase thermus |
| spellingShingle |
delignification Eucalyptus globulus biomass redox mediator thermostable bacterial laccase thermus Navas, Laura Martinez, Fernando Taverna, María E. Fetherol, Morgan Eltis, Lindsay Nicolau, Verónica V. Estenoz, Diana Campos, Eleonora Benintende, Graciela Berreta, Marcelo A thermostable laccase from Thermus sp. 2.9 and its potential for delignifcation of Eucalyptus biomass |
| topic_facet |
delignification Eucalyptus globulus biomass redox mediator thermostable bacterial laccase thermus |
| 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. |
| format |
Artículo publishedVersion Artículo |
| author |
Navas, Laura Martinez, Fernando Taverna, María E. Fetherol, Morgan Eltis, Lindsay Nicolau, Verónica V. Estenoz, Diana Campos, Eleonora Benintende, Graciela Berreta, Marcelo |
| author_facet |
Navas, Laura Martinez, Fernando Taverna, María E. Fetherol, Morgan Eltis, Lindsay Nicolau, Verónica V. Estenoz, Diana Campos, Eleonora Benintende, Graciela Berreta, Marcelo |
| author_sort |
Navas, Laura |
| title |
A thermostable laccase from Thermus sp. 2.9 and its potential for delignifcation of Eucalyptus biomass |
| title_short |
A thermostable laccase from Thermus sp. 2.9 and its potential for delignifcation of Eucalyptus biomass |
| title_full |
A thermostable laccase from Thermus sp. 2.9 and its potential for delignifcation of Eucalyptus biomass |
| title_fullStr |
A thermostable laccase from Thermus sp. 2.9 and its potential for delignifcation of Eucalyptus biomass |
| title_full_unstemmed |
A thermostable laccase from Thermus sp. 2.9 and its potential for delignifcation of Eucalyptus biomass |
| title_sort |
thermostable laccase from thermus sp. 2.9 and its potential for delignifcation of eucalyptus biomass |
| publishDate |
2019 |
| url |
http://hdl.handle.net/20.500.12272/3436 http://10.1186/s13568-019-0748-y |
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