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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.
Afiliação
  • Navas LE; Instituto de Microbiología y Zoología Agrícola, Instituto Nacional de Tecnología Agropecuaria (INTA), Nicolás Repetto y De los Reseros s/n., 1686, Hurlingham, Buenos Aires, Argentina.
  • Martínez FD; Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), CABA, Argentina.
  • Taverna ME; Instituto de Microbiología y Zoología Agrícola, Instituto Nacional de Tecnología Agropecuaria (INTA), Nicolás Repetto y De los Reseros s/n., 1686, Hurlingham, Buenos Aires, Argentina.
  • Fetherolf MM; Instituto de Desarrollo Tecnológico Para la Industria Química, INTEC (UNL-CONICET), Santa Fe, Argentina.
  • Eltis LD; GPol, UTN, Facultad Regional San Francisco, Santa Fe, Argentina.
  • Nicolau V; Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), CABA, Argentina.
  • Estenoz D; Department of Microbiology & Immunology, The University of British Columbia, Vancouver, BC, V6T 1Z3, Canada.
  • Campos E; Department of Microbiology & Immunology, The University of British Columbia, Vancouver, BC, V6T 1Z3, Canada.
  • Benintende GB; GPol, UTN, Facultad Regional San Francisco, Santa Fe, Argentina.
  • Berretta MF; Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), CABA, Argentina.
AMB Express ; 9(1): 24, 2019 Feb 12.
Article em En | MEDLINE | ID: mdl-30756202
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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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Tipo de estudo: Prognostic_studies Idioma: En Revista: AMB Express Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Argentina País de publicação: Alemanha
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Tipo de estudo: Prognostic_studies Idioma: En Revista: AMB Express Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Argentina País de publicação: Alemanha