Decolorization of Kraft liquor effluents and biochemical characterization of laccases from Phlebia brevispora BAFC 633
- Autores
- Fonseca, María Isabel; Fariña, Julia Ines; Sadañoski, Marcela Alejandra; D'Errico, Roger; Villalba, Laura Lidia; Zapata, Pedro Darío
- Año de publicación
- 2015
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Fil: Fonseca, María Isabel. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina.
Fil: Fariña, Julia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico (Tucumán). Planta Piloto de Procesos Industriales Microbiológicos. Departamento de Biotecnología Fúngica; Argentina.
Fil: Fariña, Julia Ines. Universidad Nacional de Catamarca. Facultad de Ciencias Exactas y Naturales. Cátedra de Química Biológica; Argentina.
Fil: Sadañoski, Marcela Alejandra. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina.
Fil: D'Errico, Roger. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina.
Fil: Villalba, Laura Lidia. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina.
Fil: Zapata, Pedro Darío. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina.
In this work we evaluated the decolorization ability of fungus identified as Phlebia brevispora BAFC 633 on Kraft liquor effluents and we looked at the biochemical characterization of two novel laccases from the fungus. We conducted decolorization assays on diluted Kraft liquor with the enzyme supernatants. Ligninolytic activity was demonstrated by the 20% reduction of lignin peak absorbances between 215 and 280 nm after laccase supernatants treatment. From these supernatants, two novel laccases were isolated and characterized: a constitutively expressed 60-kDa (Lac A), and a CuSO4-induced 75 kDa (Lac B). Laccases were purified by anion-exchange and gel filltration chromatography and their biochemical properties were determined. The temperature and pH optima were 70–75 °C and 4.8 for Lac A, and 60–70 °C and 4.4 for Lac B; and both exhibited high stability at low pH and high temperature. Substrate specificity of the purified enzyme was tested and the highest oxidation was to 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) with a catalytic efficiency of 2.6 × 107 s−1 mol l−1 for Lac A and 9 × 108 s−1 mol l−1 for Lac B. Enzyme supernatants can be used to remediate lignin-rich effluent. The isoenzymes tolerance to low pH and high temperature are significant features to optimize laccase production toward potential biotechnological applications. - Materia
-
Phlebia brevispora BAFC 633
Laccase isoenzymes
Biochemical characterization
Bioremediation - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- Atribución-NoComercial-CompartirIgual 4.0 Internacional
- Repositorio
- Institución
- Universidad Nacional de Misiones
- OAI Identificador
- oai:rid.unam.edu.ar:20.500.12219/4450
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Decolorization of Kraft liquor effluents and biochemical characterization of laccases from Phlebia brevispora BAFC 633Fonseca, María IsabelFariña, Julia InesSadañoski, Marcela AlejandraD'Errico, RogerVillalba, Laura LidiaZapata, Pedro DaríoPhlebia brevispora BAFC 633Laccase isoenzymesBiochemical characterizationBioremediationFil: Fonseca, María Isabel. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina.Fil: Fariña, Julia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico (Tucumán). Planta Piloto de Procesos Industriales Microbiológicos. Departamento de Biotecnología Fúngica; Argentina.Fil: Fariña, Julia Ines. Universidad Nacional de Catamarca. Facultad de Ciencias Exactas y Naturales. Cátedra de Química Biológica; Argentina.Fil: Sadañoski, Marcela Alejandra. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina.Fil: D'Errico, Roger. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina.Fil: Villalba, Laura Lidia. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina.Fil: Zapata, Pedro Darío. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina.In this work we evaluated the decolorization ability of fungus identified as Phlebia brevispora BAFC 633 on Kraft liquor effluents and we looked at the biochemical characterization of two novel laccases from the fungus. We conducted decolorization assays on diluted Kraft liquor with the enzyme supernatants. Ligninolytic activity was demonstrated by the 20% reduction of lignin peak absorbances between 215 and 280 nm after laccase supernatants treatment. From these supernatants, two novel laccases were isolated and characterized: a constitutively expressed 60-kDa (Lac A), and a CuSO4-induced 75 kDa (Lac B). Laccases were purified by anion-exchange and gel filltration chromatography and their biochemical properties were determined. The temperature and pH optima were 70–75 °C and 4.8 for Lac A, and 60–70 °C and 4.4 for Lac B; and both exhibited high stability at low pH and high temperature. Substrate specificity of the purified enzyme was tested and the highest oxidation was to 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) with a catalytic efficiency of 2.6 × 107 s−1 mol l−1 for Lac A and 9 × 108 s−1 mol l−1 for Lac B. Enzyme supernatants can be used to remediate lignin-rich effluent. The isoenzymes tolerance to low pH and high temperature are significant features to optimize laccase production toward potential biotechnological applications.Elsevier2015-10-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdf2.449 MBhttps://hdl.handle.net/20.500.12219/4450enginfo:eu-repo/semantics/altIdentifier/urn/https://www.sciencedirect.com/science/article/abs/pii/S0964830515300548info:eu-repo/semantics/openAccessAtribución-NoComercial-CompartirIgual 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-sa/4.0/reponame:Repositorio Institucional Digital de la Universidad Nacional de Misiones (UNaM)instname:Universidad Nacional de Misiones2025-09-04T11:42:44Zoai:rid.unam.edu.ar:20.500.12219/4450instacron:UNAMInstitucionalhttps://rid.unam.edu.ar/Universidad públicahttps://www.unam.edu.ar/https://rid.unam.edu.ar/oai/rsnrdArgentinaopendoar:2025-09-04 11:42:44.522Repositorio Institucional Digital de la Universidad Nacional de Misiones (UNaM) - Universidad Nacional de Misionesfalse |
dc.title.none.fl_str_mv |
Decolorization of Kraft liquor effluents and biochemical characterization of laccases from Phlebia brevispora BAFC 633 |
title |
Decolorization of Kraft liquor effluents and biochemical characterization of laccases from Phlebia brevispora BAFC 633 |
spellingShingle |
Decolorization of Kraft liquor effluents and biochemical characterization of laccases from Phlebia brevispora BAFC 633 Fonseca, María Isabel Phlebia brevispora BAFC 633 Laccase isoenzymes Biochemical characterization Bioremediation |
title_short |
Decolorization of Kraft liquor effluents and biochemical characterization of laccases from Phlebia brevispora BAFC 633 |
title_full |
Decolorization of Kraft liquor effluents and biochemical characterization of laccases from Phlebia brevispora BAFC 633 |
title_fullStr |
Decolorization of Kraft liquor effluents and biochemical characterization of laccases from Phlebia brevispora BAFC 633 |
title_full_unstemmed |
Decolorization of Kraft liquor effluents and biochemical characterization of laccases from Phlebia brevispora BAFC 633 |
title_sort |
Decolorization of Kraft liquor effluents and biochemical characterization of laccases from Phlebia brevispora BAFC 633 |
dc.creator.none.fl_str_mv |
Fonseca, María Isabel Fariña, Julia Ines Sadañoski, Marcela Alejandra D'Errico, Roger Villalba, Laura Lidia Zapata, Pedro Darío |
author |
Fonseca, María Isabel |
author_facet |
Fonseca, María Isabel Fariña, Julia Ines Sadañoski, Marcela Alejandra D'Errico, Roger Villalba, Laura Lidia Zapata, Pedro Darío |
author_role |
author |
author2 |
Fariña, Julia Ines Sadañoski, Marcela Alejandra D'Errico, Roger Villalba, Laura Lidia Zapata, Pedro Darío |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Phlebia brevispora BAFC 633 Laccase isoenzymes Biochemical characterization Bioremediation |
topic |
Phlebia brevispora BAFC 633 Laccase isoenzymes Biochemical characterization Bioremediation |
dc.description.none.fl_txt_mv |
Fil: Fonseca, María Isabel. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina. Fil: Fariña, Julia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico (Tucumán). Planta Piloto de Procesos Industriales Microbiológicos. Departamento de Biotecnología Fúngica; Argentina. Fil: Fariña, Julia Ines. Universidad Nacional de Catamarca. Facultad de Ciencias Exactas y Naturales. Cátedra de Química Biológica; Argentina. Fil: Sadañoski, Marcela Alejandra. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina. Fil: D'Errico, Roger. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina. Fil: Villalba, Laura Lidia. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina. Fil: Zapata, Pedro Darío. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina. In this work we evaluated the decolorization ability of fungus identified as Phlebia brevispora BAFC 633 on Kraft liquor effluents and we looked at the biochemical characterization of two novel laccases from the fungus. We conducted decolorization assays on diluted Kraft liquor with the enzyme supernatants. Ligninolytic activity was demonstrated by the 20% reduction of lignin peak absorbances between 215 and 280 nm after laccase supernatants treatment. From these supernatants, two novel laccases were isolated and characterized: a constitutively expressed 60-kDa (Lac A), and a CuSO4-induced 75 kDa (Lac B). Laccases were purified by anion-exchange and gel filltration chromatography and their biochemical properties were determined. The temperature and pH optima were 70–75 °C and 4.8 for Lac A, and 60–70 °C and 4.4 for Lac B; and both exhibited high stability at low pH and high temperature. Substrate specificity of the purified enzyme was tested and the highest oxidation was to 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) with a catalytic efficiency of 2.6 × 107 s−1 mol l−1 for Lac A and 9 × 108 s−1 mol l−1 for Lac B. Enzyme supernatants can be used to remediate lignin-rich effluent. The isoenzymes tolerance to low pH and high temperature are significant features to optimize laccase production toward potential biotechnological applications. |
description |
Fil: Fonseca, María Isabel. Universidad Nacional de Misiones. Facultad de Ciencias Exactas, Químicas y Naturales. Instituto de Biotecnología Misiones “Dra. María Ebe Reca”. Laboratorio de Biotecnología Molecular; Argentina. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-10-01 |
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 |
https://hdl.handle.net/20.500.12219/4450 |
url |
https://hdl.handle.net/20.500.12219/4450 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/urn/https://www.sciencedirect.com/science/article/abs/pii/S0964830515300548 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess Atribución-NoComercial-CompartirIgual 4.0 Internacional http://creativecommons.org/licenses/by-nc-sa/4.0/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
Atribución-NoComercial-CompartirIgual 4.0 Internacional http://creativecommons.org/licenses/by-nc-sa/4.0/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf 2.449 MB |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
dc.source.none.fl_str_mv |
reponame:Repositorio Institucional Digital de la Universidad Nacional de Misiones (UNaM) instname:Universidad Nacional de Misiones |
reponame_str |
Repositorio Institucional Digital de la Universidad Nacional de Misiones (UNaM) |
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Repositorio Institucional Digital de la Universidad Nacional de Misiones (UNaM) |
instname_str |
Universidad Nacional de Misiones |
repository.name.fl_str_mv |
Repositorio Institucional Digital de la Universidad Nacional de Misiones (UNaM) - Universidad Nacional de Misiones |
repository.mail.fl_str_mv |
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