Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus
- Autores
- Papinutti, Víctor Leandro; Martínez, María Jesús
- Año de publicación
- 2006
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Fomes sclerodermeus was grown on semi-defined media based on yeast extract, peptone and glucose (YPG). The fungus produced a minimum basal level of laccase activity irrespective of culture medium. The highest laccase production (20 U cm−3) was obtained in cultures supplemented with CuSO4. Manganese peroxidase (MnP) could only be detected when MnSO4 was added to the medium. None of the aromatic compounds tested stimulated further laccase or MnP production. Laccase and MnP stimulated by Cu2+ or Mn2+ respectively were purified. Two different laccase isoenzymes with the same molecular mass (67 kDa) and N-linked carbohydrate content (3%) and a slight difference in their pI values (3.41 and 3.48) were characterized. In addition, two different MnP isoenzymes with the same molecular mass (47 kDa) and N-linked carbohydrate content (4%) and different pI values (3.35 and 3.45) were characterized. Both enzymes showed good stability at 25 °C and over a wide range of pH. Both laccases oxidize ABTS (2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) more efficiently than 2,6-dimethoxyphenol (DMP) with similar efficiency values (Kcat/Km) while the MnP I, the major peroxidase isoenzyme in the studied conditions, oxidizes the Mn2+ and Mn-mediated activity on DMP more efficiently than MnP II.
Fil: Papinutti, Víctor Leandro. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental. Laboratorio de Micología Experimental; Argentina
Fil: Martínez, María Jesús. Consejo Superior de Investigaciones Científicas; España - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/29597
Ver los metadatos del registro completo
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Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeusPapinutti, Víctor LeandroMartínez, María Jesúshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Fomes sclerodermeus was grown on semi-defined media based on yeast extract, peptone and glucose (YPG). The fungus produced a minimum basal level of laccase activity irrespective of culture medium. The highest laccase production (20 U cm−3) was obtained in cultures supplemented with CuSO4. Manganese peroxidase (MnP) could only be detected when MnSO4 was added to the medium. None of the aromatic compounds tested stimulated further laccase or MnP production. Laccase and MnP stimulated by Cu2+ or Mn2+ respectively were purified. Two different laccase isoenzymes with the same molecular mass (67 kDa) and N-linked carbohydrate content (3%) and a slight difference in their pI values (3.41 and 3.48) were characterized. In addition, two different MnP isoenzymes with the same molecular mass (47 kDa) and N-linked carbohydrate content (4%) and different pI values (3.35 and 3.45) were characterized. Both enzymes showed good stability at 25 °C and over a wide range of pH. Both laccases oxidize ABTS (2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) more efficiently than 2,6-dimethoxyphenol (DMP) with similar efficiency values (Kcat/Km) while the MnP I, the major peroxidase isoenzyme in the studied conditions, oxidizes the Mn2+ and Mn-mediated activity on DMP more efficiently than MnP II.Fil: Papinutti, Víctor Leandro. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental. Laboratorio de Micología Experimental; ArgentinaFil: Martínez, María Jesús. Consejo Superior de Investigaciones Científicas; EspañaWiley2006-06-24info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/29597Papinutti, Víctor Leandro; Martínez, María Jesús; Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus; Wiley; Journal of Chemical Technology and Biotechnology; 81; 6; 24-6-2006; 1064-10700268-25751097-4660CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/jctb.1537/abstractinfo:eu-repo/semantics/altIdentifier/doi/10.1002/jctb.1537info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-17T11:04:43Zoai:ri.conicet.gov.ar:11336/29597instacron: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:34982025-09-17 11:04:43.915CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus |
| title |
Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus |
| spellingShingle |
Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus Papinutti, Víctor Leandro |
| title_short |
Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus |
| title_full |
Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus |
| title_fullStr |
Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus |
| title_full_unstemmed |
Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus |
| title_sort |
Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus |
| dc.creator.none.fl_str_mv |
Papinutti, Víctor Leandro Martínez, María Jesús |
| author |
Papinutti, Víctor Leandro |
| author_facet |
Papinutti, Víctor Leandro Martínez, María Jesús |
| author_role |
author |
| author2 |
Martínez, María Jesús |
| author2_role |
author |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
Fomes sclerodermeus was grown on semi-defined media based on yeast extract, peptone and glucose (YPG). The fungus produced a minimum basal level of laccase activity irrespective of culture medium. The highest laccase production (20 U cm−3) was obtained in cultures supplemented with CuSO4. Manganese peroxidase (MnP) could only be detected when MnSO4 was added to the medium. None of the aromatic compounds tested stimulated further laccase or MnP production. Laccase and MnP stimulated by Cu2+ or Mn2+ respectively were purified. Two different laccase isoenzymes with the same molecular mass (67 kDa) and N-linked carbohydrate content (3%) and a slight difference in their pI values (3.41 and 3.48) were characterized. In addition, two different MnP isoenzymes with the same molecular mass (47 kDa) and N-linked carbohydrate content (4%) and different pI values (3.35 and 3.45) were characterized. Both enzymes showed good stability at 25 °C and over a wide range of pH. Both laccases oxidize ABTS (2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) more efficiently than 2,6-dimethoxyphenol (DMP) with similar efficiency values (Kcat/Km) while the MnP I, the major peroxidase isoenzyme in the studied conditions, oxidizes the Mn2+ and Mn-mediated activity on DMP more efficiently than MnP II. Fil: Papinutti, Víctor Leandro. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental. Laboratorio de Micología Experimental; Argentina Fil: Martínez, María Jesús. Consejo Superior de Investigaciones Científicas; España |
| description |
Fomes sclerodermeus was grown on semi-defined media based on yeast extract, peptone and glucose (YPG). The fungus produced a minimum basal level of laccase activity irrespective of culture medium. The highest laccase production (20 U cm−3) was obtained in cultures supplemented with CuSO4. Manganese peroxidase (MnP) could only be detected when MnSO4 was added to the medium. None of the aromatic compounds tested stimulated further laccase or MnP production. Laccase and MnP stimulated by Cu2+ or Mn2+ respectively were purified. Two different laccase isoenzymes with the same molecular mass (67 kDa) and N-linked carbohydrate content (3%) and a slight difference in their pI values (3.41 and 3.48) were characterized. In addition, two different MnP isoenzymes with the same molecular mass (47 kDa) and N-linked carbohydrate content (4%) and different pI values (3.35 and 3.45) were characterized. Both enzymes showed good stability at 25 °C and over a wide range of pH. Both laccases oxidize ABTS (2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) more efficiently than 2,6-dimethoxyphenol (DMP) with similar efficiency values (Kcat/Km) while the MnP I, the major peroxidase isoenzyme in the studied conditions, oxidizes the Mn2+ and Mn-mediated activity on DMP more efficiently than MnP II. |
| publishDate |
2006 |
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2006-06-24 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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http://hdl.handle.net/11336/29597 Papinutti, Víctor Leandro; Martínez, María Jesús; Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus; Wiley; Journal of Chemical Technology and Biotechnology; 81; 6; 24-6-2006; 1064-1070 0268-2575 1097-4660 CONICET Digital CONICET |
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http://hdl.handle.net/11336/29597 |
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Papinutti, Víctor Leandro; Martínez, María Jesús; Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus; Wiley; Journal of Chemical Technology and Biotechnology; 81; 6; 24-6-2006; 1064-1070 0268-2575 1097-4660 CONICET Digital CONICET |
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eng |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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