Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements

Autores
Levin, Laura Noemí; Forchiassin, Flavia; Viale, A.
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The effects of medium components on laccase, manganese peroxidase and glyoxal oxidase production by Trametes trogii (MYA 28-11) have been studied using Plackett–Burman (PB) experimental design. Copper had the highest positive influence on ligninolytic enzyme production. T. trogii extracellular fluids obtained in the medium which rendered the highest ligninolytic production (45.32 U/ml laccase, 214.5 mU/ml manganese peroxidase and 116 mU/ml glyoxal oxidase) also showed the greatest ability to decolorize the dyes Ponceau 2R (a xylidine derivative), malachite green and anthraquinone blue (at rates of 2.14, 1.35 mg and 3 mg dye/(ml h), respectively). The relationship among decolorization rates and ligninolytic enzyme activities was analyzed by multiple regression. The results fit a linear plus interactions model. The comparison of the response surfaces obtained, suggests that while laccase activity has a greater importance in xylidine degradation, manganese peroxidase activity plays the major role in malachite green decolorization.
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: Forchiassin, Flavia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina
Fil: Viale, A.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Materia
Plackett-Burman Design
White Rot Fungi
Trametes Trogii
Dye Decolorization
Nutritional Requirements
Ligninolytic Enzymes
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:11336/46118
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/46118
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirementsLevin, Laura NoemíForchiassin, FlaviaViale, A.Plackett-Burman DesignWhite Rot FungiTrametes TrogiiDye DecolorizationNutritional RequirementsLigninolytic Enzymeshttps://purl.org/becyt/ford/1.5https://purl.org/becyt/ford/1The effects of medium components on laccase, manganese peroxidase and glyoxal oxidase production by Trametes trogii (MYA 28-11) have been studied using Plackett–Burman (PB) experimental design. Copper had the highest positive influence on ligninolytic enzyme production. T. trogii extracellular fluids obtained in the medium which rendered the highest ligninolytic production (45.32 U/ml laccase, 214.5 mU/ml manganese peroxidase and 116 mU/ml glyoxal oxidase) also showed the greatest ability to decolorize the dyes Ponceau 2R (a xylidine derivative), malachite green and anthraquinone blue (at rates of 2.14, 1.35 mg and 3 mg dye/(ml h), respectively). The relationship among decolorization rates and ligninolytic enzyme activities was analyzed by multiple regression. The results fit a linear plus interactions model. The comparison of the response surfaces obtained, suggests that while laccase activity has a greater importance in xylidine degradation, manganese peroxidase activity plays the major role in malachite green decolorization.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; ArgentinaFil: Forchiassin, Flavia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; ArgentinaFil: Viale, A.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaElsevier2005-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/46118Levin, Laura Noemí; Forchiassin, Flavia; Viale, A.; Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements; Elsevier; Process Biochemistry; 40; 3-4; 3-2005; 1381-13870032-9592CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2004.06.005info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0032959204002171info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:04:20Zoai:ri.conicet.gov.ar:11336/46118instacron: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 10:04:20.314CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements
title Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements
spellingShingle Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements
Levin, Laura Noemí
Plackett-Burman Design
White Rot Fungi
Trametes Trogii
Dye Decolorization
Nutritional Requirements
Ligninolytic Enzymes
title_short Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements
title_full Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements
title_fullStr Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements
title_full_unstemmed Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements
title_sort Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements
dc.creator.none.fl_str_mv Levin, Laura Noemí
Forchiassin, Flavia
Viale, A.
author Levin, Laura Noemí
author_facet Levin, Laura Noemí
Forchiassin, Flavia
Viale, A.
author_role author
author2 Forchiassin, Flavia
Viale, A.
author2_role author
author
dc.subject.none.fl_str_mv Plackett-Burman Design
White Rot Fungi
Trametes Trogii
Dye Decolorization
Nutritional Requirements
Ligninolytic Enzymes
topic Plackett-Burman Design
White Rot Fungi
Trametes Trogii
Dye Decolorization
Nutritional Requirements
Ligninolytic Enzymes
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.5
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The effects of medium components on laccase, manganese peroxidase and glyoxal oxidase production by Trametes trogii (MYA 28-11) have been studied using Plackett–Burman (PB) experimental design. Copper had the highest positive influence on ligninolytic enzyme production. T. trogii extracellular fluids obtained in the medium which rendered the highest ligninolytic production (45.32 U/ml laccase, 214.5 mU/ml manganese peroxidase and 116 mU/ml glyoxal oxidase) also showed the greatest ability to decolorize the dyes Ponceau 2R (a xylidine derivative), malachite green and anthraquinone blue (at rates of 2.14, 1.35 mg and 3 mg dye/(ml h), respectively). The relationship among decolorization rates and ligninolytic enzyme activities was analyzed by multiple regression. The results fit a linear plus interactions model. The comparison of the response surfaces obtained, suggests that while laccase activity has a greater importance in xylidine degradation, manganese peroxidase activity plays the major role in malachite green decolorization.
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: Forchiassin, Flavia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina
Fil: Viale, A.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
description The effects of medium components on laccase, manganese peroxidase and glyoxal oxidase production by Trametes trogii (MYA 28-11) have been studied using Plackett–Burman (PB) experimental design. Copper had the highest positive influence on ligninolytic enzyme production. T. trogii extracellular fluids obtained in the medium which rendered the highest ligninolytic production (45.32 U/ml laccase, 214.5 mU/ml manganese peroxidase and 116 mU/ml glyoxal oxidase) also showed the greatest ability to decolorize the dyes Ponceau 2R (a xylidine derivative), malachite green and anthraquinone blue (at rates of 2.14, 1.35 mg and 3 mg dye/(ml h), respectively). The relationship among decolorization rates and ligninolytic enzyme activities was analyzed by multiple regression. The results fit a linear plus interactions model. The comparison of the response surfaces obtained, suggests that while laccase activity has a greater importance in xylidine degradation, manganese peroxidase activity plays the major role in malachite green decolorization.
publishDate 2005
dc.date.none.fl_str_mv 2005-03
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/11336/46118
Levin, Laura Noemí; Forchiassin, Flavia; Viale, A.; Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements; Elsevier; Process Biochemistry; 40; 3-4; 3-2005; 1381-1387
0032-9592
CONICET Digital
CONICET
url http://hdl.handle.net/11336/46118
identifier_str_mv Levin, Laura Noemí; Forchiassin, Flavia; Viale, A.; Ligninolytic enzyme production and dye decolorization by Trametes trogii: application of the Plackett–Burman experimental design to evaluate nutritional requirements; Elsevier; Process Biochemistry; 40; 3-4; 3-2005; 1381-1387
0032-9592
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2004.06.005
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0032959204002171
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
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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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