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
Repositorio Institucional Digital de la Universidad Nacional de Misiones (UNaM)
Institución
Universidad Nacional de Misiones
OAI Identificador
oai:rid.unam.edu.ar:20.500.12219/4450

id RIDUNaM_1f58c3ab3910cf879b64d0f70884671d
oai_identifier_str oai:rid.unam.edu.ar:20.500.12219/4450
network_acronym_str RIDUNaM
repository_id_str
network_name_str Repositorio Institucional Digital de la Universidad Nacional de Misiones (UNaM)
spelling 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)
collection 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
_version_ 1842346477253296128
score 12.623145