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 Raquel; Levin, Laura Noemí; 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.
Fil: Navas, Laura Emilce. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo.; Argentina
Fil: Carballo, Romina Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; 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: Berretta, Marcelo Facundo. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo.; Argentina
Materia
AZO DYE
DECOLORIZATION
THERMOSTABLE BACTERIAL LACCASE
THERMUS SP. 2.9
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:11336/142430
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/142430
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Fast decolorization of azo dyes in alkaline solutions by a thermostable metal-tolerant bacterial laccase and proposed degradation pathwaysNavas, Laura EmilceCarballo, Romina RaquelLevin, Laura NoemíBerretta, Marcelo FacundoAZO DYEDECOLORIZATIONTHERMOSTABLE BACTERIAL LACCASETHERMUS SP. 2.9https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Biocatalytic 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.Fil: Navas, Laura Emilce. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo.; ArgentinaFil: Carballo, Romina Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; 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: Berretta, Marcelo Facundo. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo.; ArgentinaSpringer Tokyo2020-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/142430Navas, Laura Emilce; Carballo, Romina Raquel; Levin, Laura Noemí; Berretta, Marcelo Facundo; Fast decolorization of azo dyes in alkaline solutions by a thermostable metal-tolerant bacterial laccase and proposed degradation pathways; Springer Tokyo; Extremophiles; 24; 5; 7-2020; 705-7191431-0651CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00792-020-01186-winfo:eu-repo/semantics/altIdentifier/doi/10.1007/s00792-020-01186-winfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:43:52Zoai:ri.conicet.gov.ar:11336/142430instacron: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 09:43:52.648CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
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
AZO DYE
DECOLORIZATION
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 Raquel
Levin, Laura Noemí
Berretta, Marcelo Facundo
author Navas, Laura Emilce
author_facet Navas, Laura Emilce
Carballo, Romina Raquel
Levin, Laura Noemí
Berretta, Marcelo Facundo
author_role author
author2 Carballo, Romina Raquel
Levin, Laura Noemí
Berretta, Marcelo Facundo
author2_role author
author
author
dc.subject.none.fl_str_mv AZO DYE
DECOLORIZATION
THERMOSTABLE BACTERIAL LACCASE
THERMUS SP. 2.9
topic AZO DYE
DECOLORIZATION
THERMOSTABLE BACTERIAL LACCASE
THERMUS SP. 2.9
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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.
Fil: Navas, Laura Emilce. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo.; Argentina
Fil: Carballo, Romina Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; 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: Berretta, Marcelo Facundo. Instituto Nacional de Tecnologia Agropecuaria. Centro de Investigacion En Ciencias Veterinarias y Agronomicas. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo | Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Pque. Centenario. Instituto de Agrobiotecnologia y Biologia Molecular. Grupo Vinculado Instituto de Microbiologia y Zoologia Agrigola Al Iabimo.; 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
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/11336/142430
Navas, Laura Emilce; Carballo, Romina Raquel; Levin, Laura Noemí; Berretta, Marcelo Facundo; Fast decolorization of azo dyes in alkaline solutions by a thermostable metal-tolerant bacterial laccase and proposed degradation pathways; Springer Tokyo; Extremophiles; 24; 5; 7-2020; 705-719
1431-0651
CONICET Digital
CONICET
url http://hdl.handle.net/11336/142430
identifier_str_mv Navas, Laura Emilce; Carballo, Romina Raquel; Levin, Laura Noemí; Berretta, Marcelo Facundo; Fast decolorization of azo dyes in alkaline solutions by a thermostable metal-tolerant bacterial laccase and proposed degradation pathways; Springer Tokyo; Extremophiles; 24; 5; 7-2020; 705-719
1431-0651
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00792-020-01186-w
info:eu-repo/semantics/altIdentifier/doi/10.1007/s00792-020-01186-w
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
application/pdf
dc.publisher.none.fl_str_mv Springer Tokyo
publisher.none.fl_str_mv Springer Tokyo
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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