Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways

Autores
Navas, Laura Emilce; Carballo, Romina; Levin, Laura; Berretta, Marcelo Facundo
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Biocatalytic decolorization of azo dyes is hampered by their recalcitrance and the characteristics of textile effluents. Alkaline pH and heavy metals present in colored wastewaters generally limit the activity of enzymes such as laccases of fungal origin; this has led to an increasing interest in bacterial laccases. In this work, the dye decolorization ability of LAC_2.9, a laccase from the thermophilic bacterial strain Thermus sp. 2.9, was investigated. Its resistance towards different pHs and toxic heavy metals frequently present in wastewaters was also characterized. LAC_2.9 was active and highly stable in the pH range of 5.0 to 9.0. Even at 100 mM Cd+2, As+5 and Ni+2 LAC_2.9 retained 99%, 86% and 75% of its activity, respectively. LAC_2.9 was capable of decolorizing 98% of Xylidine, 54% of RBBR, 40% of Gentian Violet, and 33% of Methyl Orange after 24 h incubation at pH 9, at 60 °C, without the addition of redox mediators. At acidic pH, the presence of the mediator 1-hydroxybenzotriazole generally increased the catalytic effectiveness. We analyzed the degradation products of laccase-treated Xylidine and Methyl Orange by capillary electrophoresis and mass spectrometry, and propose a degradation pathway for these dyes. For its ability to decolorize recalcitrant dyes, at pH 9, and its stability under the tested conditions, LAC_2.9 could be effectively used to decolorize azo dyes in alkaline and heavy metal containing effluents.
Instituto de Microbiología y Zoología Agrícola (IMYZA)
Fil: Navas, Laura Emilce. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Navas, Laura Emilce. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Carballo, Romina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológicas; Argentina
Fil: Carballo, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Levin, Laura Noemí. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Levin, Laura Noemí. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental, Instituto de Micología y Botánica; Argentina
Fil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Berretta, Marcelo Facundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fuente
Extremophiles 24 : 705-719 (2020)
Materia
Solución
Proceso de Decoloración
Colorantes Azóicos
Solutions
Decolorization
Azo Dyes
Thermostable Bacterial Laccase
Thermus sp. 2.9
Nivel de accesibilidad
acceso restringido
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/13889
Acceder
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oai_identifier_str oai:localhost:20.500.12123/13889
network_acronym_str INTADig
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network_name_str INTA Digital (INTA)
spelling Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathwaysNavas, Laura EmilceCarballo, RominaLevin, LauraBerretta, Marcelo FacundoSoluciónProceso de DecoloraciónColorantes AzóicosSolutionsDecolorizationAzo DyesThermostable Bacterial LaccaseThermus sp. 2.9Biocatalytic decolorization of azo dyes is hampered by their recalcitrance and the characteristics of textile effluents. Alkaline pH and heavy metals present in colored wastewaters generally limit the activity of enzymes such as laccases of fungal origin; this has led to an increasing interest in bacterial laccases. In this work, the dye decolorization ability of LAC_2.9, a laccase from the thermophilic bacterial strain Thermus sp. 2.9, was investigated. Its resistance towards different pHs and toxic heavy metals frequently present in wastewaters was also characterized. LAC_2.9 was active and highly stable in the pH range of 5.0 to 9.0. Even at 100 mM Cd+2, As+5 and Ni+2 LAC_2.9 retained 99%, 86% and 75% of its activity, respectively. LAC_2.9 was capable of decolorizing 98% of Xylidine, 54% of RBBR, 40% of Gentian Violet, and 33% of Methyl Orange after 24 h incubation at pH 9, at 60 °C, without the addition of redox mediators. At acidic pH, the presence of the mediator 1-hydroxybenzotriazole generally increased the catalytic effectiveness. We analyzed the degradation products of laccase-treated Xylidine and Methyl Orange by capillary electrophoresis and mass spectrometry, and propose a degradation pathway for these dyes. For its ability to decolorize recalcitrant dyes, at pH 9, and its stability under the tested conditions, LAC_2.9 could be effectively used to decolorize azo dyes in alkaline and heavy metal containing effluents.Instituto de Microbiología y Zoología Agrícola (IMYZA)Fil: Navas, Laura Emilce. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; ArgentinaFil: Navas, Laura Emilce. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Agrobiotecnología y Biología Molecular; ArgentinaFil: Carballo, Romina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológicas; ArgentinaFil: Carballo, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Levin, Laura Noemí. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Levin, Laura Noemí. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental, Instituto de Micología y Botánica; ArgentinaFil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; ArgentinaFil: Berretta, Marcelo Facundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Agrobiotecnología y Biología Molecular; ArgentinaSpringer2023-01-12T09:08:11Z2023-01-12T09:08:11Z2020-07-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/13889https://link.springer.com/article/10.1007/s00792-020-01186-w1431-06511433-4909https://doi.org/10.1007/s00792-020-01186-wExtremophiles 24 : 705-719 (2020)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repograntAgreement/INTA/PNAIyAV-1130034/AR./Desarrollo de procesos para la transformación de biomasa en bioenergía.info:eu-repo/semantics/restrictedAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2025-09-04T09:49:28Zoai:localhost:20.500.12123/13889instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-04 09:49:28.613INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways
title Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways
spellingShingle Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways
Navas, Laura Emilce
Solución
Proceso de Decoloración
Colorantes Azóicos
Solutions
Decolorization
Azo Dyes
Thermostable Bacterial Laccase
Thermus sp. 2.9
title_short Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways
title_full Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways
title_fullStr Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways
title_full_unstemmed Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways
title_sort Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways
dc.creator.none.fl_str_mv Navas, Laura Emilce
Carballo, Romina
Levin, Laura
Berretta, Marcelo Facundo
author Navas, Laura Emilce
author_facet Navas, Laura Emilce
Carballo, Romina
Levin, Laura
Berretta, Marcelo Facundo
author_role author
author2 Carballo, Romina
Levin, Laura
Berretta, Marcelo Facundo
author2_role author
author
author
dc.subject.none.fl_str_mv Solución
Proceso de Decoloración
Colorantes Azóicos
Solutions
Decolorization
Azo Dyes
Thermostable Bacterial Laccase
Thermus sp. 2.9
topic Solución
Proceso de Decoloración
Colorantes Azóicos
Solutions
Decolorization
Azo Dyes
Thermostable Bacterial Laccase
Thermus sp. 2.9
dc.description.none.fl_txt_mv Biocatalytic decolorization of azo dyes is hampered by their recalcitrance and the characteristics of textile effluents. Alkaline pH and heavy metals present in colored wastewaters generally limit the activity of enzymes such as laccases of fungal origin; this has led to an increasing interest in bacterial laccases. In this work, the dye decolorization ability of LAC_2.9, a laccase from the thermophilic bacterial strain Thermus sp. 2.9, was investigated. Its resistance towards different pHs and toxic heavy metals frequently present in wastewaters was also characterized. LAC_2.9 was active and highly stable in the pH range of 5.0 to 9.0. Even at 100 mM Cd+2, As+5 and Ni+2 LAC_2.9 retained 99%, 86% and 75% of its activity, respectively. LAC_2.9 was capable of decolorizing 98% of Xylidine, 54% of RBBR, 40% of Gentian Violet, and 33% of Methyl Orange after 24 h incubation at pH 9, at 60 °C, without the addition of redox mediators. At acidic pH, the presence of the mediator 1-hydroxybenzotriazole generally increased the catalytic effectiveness. We analyzed the degradation products of laccase-treated Xylidine and Methyl Orange by capillary electrophoresis and mass spectrometry, and propose a degradation pathway for these dyes. For its ability to decolorize recalcitrant dyes, at pH 9, and its stability under the tested conditions, LAC_2.9 could be effectively used to decolorize azo dyes in alkaline and heavy metal containing effluents.
Instituto de Microbiología y Zoología Agrícola (IMYZA)
Fil: Navas, Laura Emilce. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Navas, Laura Emilce. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Carballo, Romina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológicas; Argentina
Fil: Carballo, Romina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Levin, Laura Noemí. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Levin, Laura Noemí. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental, Instituto de Micología y Botánica; Argentina
Fil: Berretta, Marcelo Facundo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina
Fil: Berretta, Marcelo Facundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Agrobiotecnología y Biología Molecular; Argentina
description Biocatalytic decolorization of azo dyes is hampered by their recalcitrance and the characteristics of textile effluents. Alkaline pH and heavy metals present in colored wastewaters generally limit the activity of enzymes such as laccases of fungal origin; this has led to an increasing interest in bacterial laccases. In this work, the dye decolorization ability of LAC_2.9, a laccase from the thermophilic bacterial strain Thermus sp. 2.9, was investigated. Its resistance towards different pHs and toxic heavy metals frequently present in wastewaters was also characterized. LAC_2.9 was active and highly stable in the pH range of 5.0 to 9.0. Even at 100 mM Cd+2, As+5 and Ni+2 LAC_2.9 retained 99%, 86% and 75% of its activity, respectively. LAC_2.9 was capable of decolorizing 98% of Xylidine, 54% of RBBR, 40% of Gentian Violet, and 33% of Methyl Orange after 24 h incubation at pH 9, at 60 °C, without the addition of redox mediators. At acidic pH, the presence of the mediator 1-hydroxybenzotriazole generally increased the catalytic effectiveness. We analyzed the degradation products of laccase-treated Xylidine and Methyl Orange by capillary electrophoresis and mass spectrometry, and propose a degradation pathway for these dyes. For its ability to decolorize recalcitrant dyes, at pH 9, and its stability under the tested conditions, LAC_2.9 could be effectively used to decolorize azo dyes in alkaline and heavy metal containing effluents.
publishDate 2020
dc.date.none.fl_str_mv 2020-07-02
2023-01-12T09:08:11Z
2023-01-12T09:08:11Z
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/20.500.12123/13889
https://link.springer.com/article/10.1007/s00792-020-01186-w
1431-0651
1433-4909
https://doi.org/10.1007/s00792-020-01186-w
url http://hdl.handle.net/20.500.12123/13889
https://link.springer.com/article/10.1007/s00792-020-01186-w
https://doi.org/10.1007/s00792-020-01186-w
identifier_str_mv 1431-0651
1433-4909
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repograntAgreement/INTA/PNAIyAV-1130034/AR./Desarrollo de procesos para la transformación de biomasa en bioenergía.
dc.rights.none.fl_str_mv info:eu-repo/semantics/restrictedAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv restrictedAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv Extremophiles 24 : 705-719 (2020)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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