Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus
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...
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2006
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02682575_v81_n6_p1064_Papinutti http://hdl.handle.net/20.500.12110/paper_02682575_v81_n6_p1064_Papinutti |
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paper:paper_02682575_v81_n6_p1064_Papinutti2023-06-08T15:24:11Z Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus Aromatic compounds Fomes sclerodermeus Laccase Manganese peroxidase Purification Aromatic compounds Carbohydrates Characterization Enzymes Glucose Lignin pH Proteins Purification Fomes sclerodermeus Laccase Manganese peroxidase Fungi 2,2' azino bis(3 ethylbenzthiazoline 6 sulfonic acid) aromatic compound carbohydrate copper sulfate glucose isoenzyme laccase lignin manganese peroxidase manganese sulfate peptone phenol derivative syringol thiazole derivative unclassified drug Aromatic compounds Carbohydrates Characterization Enzymes Fungi Glucose Lignin pH Proteins Purification article carbohydrate analysis controlled study culture medium enzyme activity enzyme analysis enzyme metabolism enzyme purification enzyme stability enzyme synthesis Fomes sclerodermeus fungus molecular weight nonhuman pH measurement temperature measurement Fomes Fungi 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 (30%) 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 1, the major peroxidase isoenzyme in the studied conditions, oxidizes the Mn2+ and Mn-mediated activity on DMP more efficiently than MnP II. © 2006 Society of Chemical Industry. 2006 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02682575_v81_n6_p1064_Papinutti http://hdl.handle.net/20.500.12110/paper_02682575_v81_n6_p1064_Papinutti |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Aromatic compounds Fomes sclerodermeus Laccase Manganese peroxidase Purification Aromatic compounds Carbohydrates Characterization Enzymes Glucose Lignin pH Proteins Purification Fomes sclerodermeus Laccase Manganese peroxidase Fungi 2,2' azino bis(3 ethylbenzthiazoline 6 sulfonic acid) aromatic compound carbohydrate copper sulfate glucose isoenzyme laccase lignin manganese peroxidase manganese sulfate peptone phenol derivative syringol thiazole derivative unclassified drug Aromatic compounds Carbohydrates Characterization Enzymes Fungi Glucose Lignin pH Proteins Purification article carbohydrate analysis controlled study culture medium enzyme activity enzyme analysis enzyme metabolism enzyme purification enzyme stability enzyme synthesis Fomes sclerodermeus fungus molecular weight nonhuman pH measurement temperature measurement Fomes Fungi |
| spellingShingle |
Aromatic compounds Fomes sclerodermeus Laccase Manganese peroxidase Purification Aromatic compounds Carbohydrates Characterization Enzymes Glucose Lignin pH Proteins Purification Fomes sclerodermeus Laccase Manganese peroxidase Fungi 2,2' azino bis(3 ethylbenzthiazoline 6 sulfonic acid) aromatic compound carbohydrate copper sulfate glucose isoenzyme laccase lignin manganese peroxidase manganese sulfate peptone phenol derivative syringol thiazole derivative unclassified drug Aromatic compounds Carbohydrates Characterization Enzymes Fungi Glucose Lignin pH Proteins Purification article carbohydrate analysis controlled study culture medium enzyme activity enzyme analysis enzyme metabolism enzyme purification enzyme stability enzyme synthesis Fomes sclerodermeus fungus molecular weight nonhuman pH measurement temperature measurement Fomes Fungi Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus |
| topic_facet |
Aromatic compounds Fomes sclerodermeus Laccase Manganese peroxidase Purification Aromatic compounds Carbohydrates Characterization Enzymes Glucose Lignin pH Proteins Purification Fomes sclerodermeus Laccase Manganese peroxidase Fungi 2,2' azino bis(3 ethylbenzthiazoline 6 sulfonic acid) aromatic compound carbohydrate copper sulfate glucose isoenzyme laccase lignin manganese peroxidase manganese sulfate peptone phenol derivative syringol thiazole derivative unclassified drug Aromatic compounds Carbohydrates Characterization Enzymes Fungi Glucose Lignin pH Proteins Purification article carbohydrate analysis controlled study culture medium enzyme activity enzyme analysis enzyme metabolism enzyme purification enzyme stability enzyme synthesis Fomes sclerodermeus fungus molecular weight nonhuman pH measurement temperature measurement Fomes Fungi |
| 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 (30%) 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 1, the major peroxidase isoenzyme in the studied conditions, oxidizes the Mn2+ and Mn-mediated activity on DMP more efficiently than MnP II. © 2006 Society of Chemical Industry. |
| title |
Production and characterization of laccase and manganese peroxidase from the ligninolytic fungus Fomes sclerodermeus |
| 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 |
| publishDate |
2006 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02682575_v81_n6_p1064_Papinutti http://hdl.handle.net/20.500.12110/paper_02682575_v81_n6_p1064_Papinutti |
| _version_ |
1768543466123427840 |