Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways
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 ba...
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| Format: | info:ar-repo/semantics/artículo |
| Language: | Inglés |
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Springer
2023
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| Online Access: | 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 |
| _version_ | 1855036761145606144 |
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| author | Navas, Laura Emilce Carballo, Romina Levin, Laura Berretta, Marcelo Facundo |
| author_browse | Berretta, Marcelo Facundo Carballo, Romina Levin, Laura Navas, Laura Emilce |
| author_facet | Navas, Laura Emilce Carballo, Romina Levin, Laura Berretta, Marcelo Facundo |
| author_sort | Navas, Laura Emilce |
| collection | INTA Digital |
| 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. |
| format | info:ar-repo/semantics/artículo |
| id | INTA13889 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2023 |
| publishDateRange | 2023 |
| publishDateSort | 2023 |
| publisher | Springer |
| publisherStr | Springer |
| record_format | dspace |
| spelling | INTA138892023-01-12T09:29:00Z Fast decolorization of azo dyes in alkaline solutions by a thermostable metal‑tolerant bacterial laccase and proposed degradation pathways Navas, Laura Emilce Carballo, Romina Levin, Laura Berretta, Marcelo Facundo Solución Proceso de Decoloración Colorantes Azóicos Solutions Decolorization Azo Dyes Thermostable Bacterial Laccase Thermus sp. 2.9 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 2023-01-12T09:08:11Z 2023-01-12T09:08:11Z 2020-07-02 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 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 eng info:eu-repograntAgreement/INTA/PNAIyAV-1130034/AR./Desarrollo de procesos para la transformación de biomasa en bioenergía. 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) application/pdf Springer Extremophiles 24 : 705-719 (2020) |
| spellingShingle | Solución Proceso de Decoloración Colorantes Azóicos Solutions Decolorization Azo Dyes Thermostable Bacterial Laccase Thermus sp. 2.9 Navas, Laura Emilce Carballo, Romina Levin, Laura Berretta, Marcelo Facundo 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 |
| 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_short | 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 |
| topic | Solución Proceso de Decoloración Colorantes Azóicos Solutions Decolorization Azo Dyes Thermostable Bacterial Laccase Thermus sp. 2.9 |
| 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 |
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