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

Autores
Campos, Paula Andrea; Levin, Laura Noemí; Wirth, Sonia Alejandra
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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 minutes 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.
Fil: Campos, Paula Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
Fil: Levin, Laura Noemí. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Micología y Botánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Micología y Botánica; Argentina
Fil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
Materia
Acetosyringone
Dye Decolorization
Pichia Pastoris
Thermostable Laccase
Trametes Trogii
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/26478
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/26478
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463Campos, Paula AndreaLevin, Laura NoemíWirth, Sonia AlejandraAcetosyringoneDye DecolorizationPichia PastorisThermostable LaccaseTrametes Trogiihttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Laccases 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 minutes 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.Fil: Campos, Paula Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; ArgentinaFil: Levin, Laura Noemí. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Micología y Botánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Micología y Botánica; ArgentinaFil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; ArgentinaElsevier2015-03-25info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/26478Campos, Paula Andrea; Levin, Laura Noemí; Wirth, Sonia Alejandra; Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463; Elsevier; Process Biochemistry; 51; 7; 25-3-2015; 895-9031359-51131873-3298CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1359511316300459info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2016.03.015info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:03:00Zoai:ri.conicet.gov.ar:11336/26478instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:03:01.005CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
title Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
spellingShingle Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
Campos, Paula Andrea
Acetosyringone
Dye Decolorization
Pichia Pastoris
Thermostable Laccase
Trametes Trogii
title_short Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
title_full Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
title_fullStr Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
title_full_unstemmed Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
title_sort Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463
dc.creator.none.fl_str_mv Campos, Paula Andrea
Levin, Laura Noemí
Wirth, Sonia Alejandra
author Campos, Paula Andrea
author_facet Campos, Paula Andrea
Levin, Laura Noemí
Wirth, Sonia Alejandra
author_role author
author2 Levin, Laura Noemí
Wirth, Sonia Alejandra
author2_role author
author
dc.subject.none.fl_str_mv Acetosyringone
Dye Decolorization
Pichia Pastoris
Thermostable Laccase
Trametes Trogii
topic Acetosyringone
Dye Decolorization
Pichia Pastoris
Thermostable Laccase
Trametes Trogii
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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 minutes 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.
Fil: Campos, Paula Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
Fil: Levin, Laura Noemí. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Micología y Botánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Micología y Botánica; Argentina
Fil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
description 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 minutes 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.
publishDate 2015
dc.date.none.fl_str_mv 2015-03-25
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/26478
Campos, Paula Andrea; Levin, Laura Noemí; Wirth, Sonia Alejandra; Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463; Elsevier; Process Biochemistry; 51; 7; 25-3-2015; 895-903
1359-5113
1873-3298
CONICET Digital
CONICET
url http://hdl.handle.net/11336/26478
identifier_str_mv Campos, Paula Andrea; Levin, Laura Noemí; Wirth, Sonia Alejandra; Heterologous production, characterization and dye decolorization ability of a novel thermostable laccase isoenzyme from Trametes trogii BAFC 463; Elsevier; Process Biochemistry; 51; 7; 25-3-2015; 895-903
1359-5113
1873-3298
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1359511316300459
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2016.03.015
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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