Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase

Autores
Britos, Claudia Noelia; Gianolini, Julián Emilio; Portillo, Hugo Gabriel; Trelles, Jorge Abel
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Several industrial activities release highly recalcitrant and dangerous dyes into the environment. The use of laccases to catalyze biooxidations represents an important alternative to dye effluent treatments. This study reports on the characterization of extracellular laccase of P. vulgaris ATCC 6896. This new enzyme was stable for more than 6h at 60°C and retained its activity completely under acidic and alkaline conditions. The P. vulgaris laccase showed a high tolerance to enzymatic inhibitors such as sodium azide and organic solvents (acetonitrile, ethanol and methanol), and its activity increased up to 5 times with the addition of Fe2+,Cu2+,Zn2+ or surfactants. Finally, the P. vulgaris laccase was stabilized by immobilization in Cu-alginate gels. The derivatives showed significantly higher thermostability than the free enzyme, and extended shelf life of up to 500h. This biocatalyst was used to decolorize bromothymol blue (59%), Coomassie brilliant blue R (72%), methyl violet 10B (52%), Remazol brilliant blue R (51%) and trypan blue (85%) at short reaction times without the addition of mediators, and reused up to 160 cycles without loss of efficiency. This enzymatic biocatalyst could be effectively used in sewage treatment due to its ability to decolorize recalcitrant dyes without the addition of redox mediators, and its high thermal and chemical stability.
Fil: Britos, Claudia Noelia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Gianolini, Julián Emilio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Portillo, Hugo Gabriel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Trelles, Jorge Abel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Materia
BIODEGRADATION
LACCASE
DYES
IMMOBILIZATION
BIOCATALYSIS
CU-ALGINATE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/155470
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/155470
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccaseBritos, Claudia NoeliaGianolini, Julián EmilioPortillo, Hugo GabrielTrelles, Jorge AbelBIODEGRADATIONLACCASEDYESIMMOBILIZATIONBIOCATALYSISCU-ALGINATEhttps://purl.org/becyt/ford/2.8https://purl.org/becyt/ford/2Several industrial activities release highly recalcitrant and dangerous dyes into the environment. The use of laccases to catalyze biooxidations represents an important alternative to dye effluent treatments. This study reports on the characterization of extracellular laccase of P. vulgaris ATCC 6896. This new enzyme was stable for more than 6h at 60°C and retained its activity completely under acidic and alkaline conditions. The P. vulgaris laccase showed a high tolerance to enzymatic inhibitors such as sodium azide and organic solvents (acetonitrile, ethanol and methanol), and its activity increased up to 5 times with the addition of Fe2+,Cu2+,Zn2+ or surfactants. Finally, the P. vulgaris laccase was stabilized by immobilization in Cu-alginate gels. The derivatives showed significantly higher thermostability than the free enzyme, and extended shelf life of up to 500h. This biocatalyst was used to decolorize bromothymol blue (59%), Coomassie brilliant blue R (72%), methyl violet 10B (52%), Remazol brilliant blue R (51%) and trypan blue (85%) at short reaction times without the addition of mediators, and reused up to 160 cycles without loss of efficiency. This enzymatic biocatalyst could be effectively used in sewage treatment due to its ability to decolorize recalcitrant dyes without the addition of redox mediators, and its high thermal and chemical stability.Fil: Britos, Claudia Noelia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; ArgentinaFil: Gianolini, Julián Emilio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; ArgentinaFil: Portillo, Hugo Gabriel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; ArgentinaFil: Trelles, Jorge Abel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; ArgentinaElsevier2018-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/155470Britos, Claudia Noelia; Gianolini, Julián Emilio; Portillo, Hugo Gabriel; Trelles, Jorge Abel; Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase; Elsevier; Biocatalysis and Agricultural Biotechnology; 14; 3-2018; 221-2271878-8181CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcab.2018.03.015info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1878818117305935info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:46:45Zoai:ri.conicet.gov.ar:11336/155470instacron: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:34982025-09-29 10:46:45.823CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase
title Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase
spellingShingle Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase
Britos, Claudia Noelia
BIODEGRADATION
LACCASE
DYES
IMMOBILIZATION
BIOCATALYSIS
CU-ALGINATE
title_short Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase
title_full Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase
title_fullStr Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase
title_full_unstemmed Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase
title_sort Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase
dc.creator.none.fl_str_mv Britos, Claudia Noelia
Gianolini, Julián Emilio
Portillo, Hugo Gabriel
Trelles, Jorge Abel
author Britos, Claudia Noelia
author_facet Britos, Claudia Noelia
Gianolini, Julián Emilio
Portillo, Hugo Gabriel
Trelles, Jorge Abel
author_role author
author2 Gianolini, Julián Emilio
Portillo, Hugo Gabriel
Trelles, Jorge Abel
author2_role author
author
author
dc.subject.none.fl_str_mv BIODEGRADATION
LACCASE
DYES
IMMOBILIZATION
BIOCATALYSIS
CU-ALGINATE
topic BIODEGRADATION
LACCASE
DYES
IMMOBILIZATION
BIOCATALYSIS
CU-ALGINATE
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.8
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Several industrial activities release highly recalcitrant and dangerous dyes into the environment. The use of laccases to catalyze biooxidations represents an important alternative to dye effluent treatments. This study reports on the characterization of extracellular laccase of P. vulgaris ATCC 6896. This new enzyme was stable for more than 6h at 60°C and retained its activity completely under acidic and alkaline conditions. The P. vulgaris laccase showed a high tolerance to enzymatic inhibitors such as sodium azide and organic solvents (acetonitrile, ethanol and methanol), and its activity increased up to 5 times with the addition of Fe2+,Cu2+,Zn2+ or surfactants. Finally, the P. vulgaris laccase was stabilized by immobilization in Cu-alginate gels. The derivatives showed significantly higher thermostability than the free enzyme, and extended shelf life of up to 500h. This biocatalyst was used to decolorize bromothymol blue (59%), Coomassie brilliant blue R (72%), methyl violet 10B (52%), Remazol brilliant blue R (51%) and trypan blue (85%) at short reaction times without the addition of mediators, and reused up to 160 cycles without loss of efficiency. This enzymatic biocatalyst could be effectively used in sewage treatment due to its ability to decolorize recalcitrant dyes without the addition of redox mediators, and its high thermal and chemical stability.
Fil: Britos, Claudia Noelia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Gianolini, Julián Emilio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Portillo, Hugo Gabriel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
Fil: Trelles, Jorge Abel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Investigación en Biotecnología Sustentable; Argentina
description Several industrial activities release highly recalcitrant and dangerous dyes into the environment. The use of laccases to catalyze biooxidations represents an important alternative to dye effluent treatments. This study reports on the characterization of extracellular laccase of P. vulgaris ATCC 6896. This new enzyme was stable for more than 6h at 60°C and retained its activity completely under acidic and alkaline conditions. The P. vulgaris laccase showed a high tolerance to enzymatic inhibitors such as sodium azide and organic solvents (acetonitrile, ethanol and methanol), and its activity increased up to 5 times with the addition of Fe2+,Cu2+,Zn2+ or surfactants. Finally, the P. vulgaris laccase was stabilized by immobilization in Cu-alginate gels. The derivatives showed significantly higher thermostability than the free enzyme, and extended shelf life of up to 500h. This biocatalyst was used to decolorize bromothymol blue (59%), Coomassie brilliant blue R (72%), methyl violet 10B (52%), Remazol brilliant blue R (51%) and trypan blue (85%) at short reaction times without the addition of mediators, and reused up to 160 cycles without loss of efficiency. This enzymatic biocatalyst could be effectively used in sewage treatment due to its ability to decolorize recalcitrant dyes without the addition of redox mediators, and its high thermal and chemical stability.
publishDate 2018
dc.date.none.fl_str_mv 2018-03
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/11336/155470
Britos, Claudia Noelia; Gianolini, Julián Emilio; Portillo, Hugo Gabriel; Trelles, Jorge Abel; Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase; Elsevier; Biocatalysis and Agricultural Biotechnology; 14; 3-2018; 221-227
1878-8181
CONICET Digital
CONICET
url http://hdl.handle.net/11336/155470
identifier_str_mv Britos, Claudia Noelia; Gianolini, Julián Emilio; Portillo, Hugo Gabriel; Trelles, Jorge Abel; Biodegradation of industrial dyes by a solvent, metal and surfactant-stable extracellular bacterial laccase; Elsevier; Biocatalysis and Agricultural Biotechnology; 14; 3-2018; 221-227
1878-8181
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcab.2018.03.015
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1878818117305935
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
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 13.070432

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