Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463

Laccases are multicopper polyphenol oxidases that are able to catalyze the oxidation of a wide range of phenolic compounds with the simultaneous reduction of O2 to H2O. Despite their promising industrial uses, feasible incorporation of laccases in harsh processes requires the bioprospecting and/or e...

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Autor principal: Campos, P.A
Otros Autores: Levin, L.N, Wirth, S.A
Formato: Capítulo de libro
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Publicado: Elsevier Ltd 2016
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030 |a PBCHE 
100 1 |a Campos, P.A. 
245 1 0 |a Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463 
260 |b Elsevier Ltd  |c 2016 
270 1 0 |m Wirth, S.A.; Laboratorio de Agrobiotecnología, Departamento de Fisiología Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, IBBEA-CONICET-UBA, Pabellón 2 Ciudad Universitaria, Piso 2, Argentina; email: sonia.wirth@gmail.com 
506 |2 openaire  |e Política editorial 
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520 3 |a Laccases are multicopper polyphenol oxidases that are able to catalyze the oxidation of a wide range of phenolic compounds with the simultaneous reduction of O2 to H2O. Despite their promising industrial uses, feasible incorporation of laccases in harsh processes requires the bioprospecting and/or engineering of enzymes to be stable and active in acidic or alkaline pHs, high temperatures, oxidative conditions and tolerant to high salinity and/or organic solvents. Here we used a PCR-based screening to clone two novel laccase coding sequences from the white-rot basidiomycete Trametes trogii. Recombinant expression of lcc3 gene in Komagataella (=Pichia) pastoris showed that it encodes a thermo active and thermostable laccase with an optimum temperature of 50 °C and with a half-life of 45 min at 70 °C and a stability higher than 3 h at 60 °C. Furthermore, recombinant LCC3 was capable of decolorizing between 50% and 100% of indigoid, triarylmethane, azoic and anthraquinonic synthetic dyes in the presence of the natural redox mediator acetosyringone within 2 h of incubation at pH 6 and 70 °C. © 2016 Elsevier Ltd.  |l eng 
593 |a Laboratorio de Agrobiotecnología, Departamento de Fisiología Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, IBBEA-CONICET-UBA, Pabellón 2 Ciudad Universitaria, Piso 2, Buenos Aires, C1428EGA, Argentina 
593 |a Laboratorio de Micología Experimental, Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, PROPLAME-PRHIDEB-CONICET, Pabellón 2 Ciudad Universitaria, Piso 4, Buenos Aires, C1428EGA, Argentina 
690 1 0 |a ACETOSYRINGONE 
690 1 0 |a DYE DECOLORIZATION 
690 1 0 |a PICHIA PASTORIS 
690 1 0 |a THERMOSTABLE LACCASE 
690 1 0 |a TRAMETES TROGII 
690 1 0 |a ALKALINITY 
690 1 0 |a C (PROGRAMMING LANGUAGE) 
690 1 0 |a GENE EXPRESSION 
690 1 0 |a ACETOSYRINGONE 
690 1 0 |a DYE DECOLORIZATION 
690 1 0 |a LACCASES 
690 1 0 |a PICHIA PASTORIS 
690 1 0 |a TRAMETES TROGII 
690 1 0 |a ENZYMES 
700 1 |a Levin, L.N. 
700 1 |a Wirth, S.A. 
773 0 |d Elsevier Ltd, 2016  |g v. 51  |h pp. 895-903  |k n. 7  |p Process Biochem.  |x 13595113  |t Process Biochemistry 
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