- Library Home /
- Search Collections /
- Open Collections /
- Browse Collections /
- UBC Faculty Research and Publications /
- A thermostable laccase from Thermus sp. 2.9 and its...
Open Collections
UBC Faculty Research and Publications
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
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 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.
Item Metadata
Title |
A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass
|
Creator | |
Publisher |
Springer Berlin Heidelberg
|
Date Issued |
2019-02-12
|
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.
|
Subject | |
Genre | |
Type | |
Language |
eng
|
Date Available |
2019-02-13
|
Provider |
Vancouver : University of British Columbia Library
|
Rights |
Attribution 4.0 International (CC BY 4.0)
|
DOI |
10.14288/1.0376435
|
URI | |
Affiliation | |
Citation |
AMB Express. 2019 Feb 12;9(1):24
|
Publisher DOI |
10.1186/s13568-019-0748-y
|
Peer Review Status |
Reviewed
|
Scholarly Level |
Faculty
|
Copyright Holder |
The Author(s)
|
Rights URI | |
Aggregated Source Repository |
DSpace
|
Item Media
Item Citations and Data
Rights
Attribution 4.0 International (CC BY 4.0)