Purification and characterization of an extracellular endo-1,4-β-xylanase from Fusarium oxysporum f. sp. melonis
Fusarium oxysporum f. sp. melonis produces extracellular endo-1,4-β-xylanase and β-xylosidase when grown in shaken culture at 26°C in a mineral salts medium containing oat spelt xylan and glucose as carbon sources. Endo-1,4-β-xylanase was purified 251 times from 5-day-old culture filtrates, by Sepha...
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todo:paper_03781097_v118_n3_p305_Alconada2023-10-03T15:31:38Z Purification and characterization of an extracellular endo-1,4-β-xylanase from Fusarium oxysporum f. sp. melonis Alconada, T.M. Martínez, M.J. Endo-1,4-β-xylanase activity Fusarium oxysporum f. sp. melonis β-Xylosidase activity endo 1,4 beta xylanase unclassified drug xylan article enzyme activity enzyme purification fusarium oxysporum high performance liquid chromatography nonhuman ph polyacrylamide gel electrophoresis priority journal Carbohydrates Culture Media Fusarium Glycoside Hydrolases Metals Molecular Weight Fusarium oxysporum f. sp. melonis Fusarium sp. Melonis Triticum aestivum subsp. spelta Fusarium oxysporum f. sp. melonis produces extracellular endo-1,4-β-xylanase and β-xylosidase when grown in shaken culture at 26°C in a mineral salts medium containing oat spelt xylan and glucose as carbon sources. Endo-1,4-β-xylanase was purified 251 times from 5-day-old culture filtrates, by Sephacryl S-200, ion exchange and gel filtration HPLC. The purified sample yielded a single band in SDS polyacrylamide gels with a molecular mass of 80 kDa on electrophoretic mobility and 83 kDa by gel filtration behavior. High activity of the endo-1,4-β-xylanase against xylan was observed between 5 and 8 pH, and between 40 and 60°C, the optimum pH and temperature being 5.0 and 50°C, respectively. Kinetic properties of the enzyme are similar to those of other fungal xylanases, showing high affinity towards oat spelt xylan with a Km of 1 mM expressed as xylose equivalent. © 1994. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03781097_v118_n3_p305_Alconada |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Endo-1,4-β-xylanase activity Fusarium oxysporum f. sp. melonis β-Xylosidase activity endo 1,4 beta xylanase unclassified drug xylan article enzyme activity enzyme purification fusarium oxysporum high performance liquid chromatography nonhuman ph polyacrylamide gel electrophoresis priority journal Carbohydrates Culture Media Fusarium Glycoside Hydrolases Metals Molecular Weight Fusarium oxysporum f. sp. melonis Fusarium sp. Melonis Triticum aestivum subsp. spelta |
| spellingShingle |
Endo-1,4-β-xylanase activity Fusarium oxysporum f. sp. melonis β-Xylosidase activity endo 1,4 beta xylanase unclassified drug xylan article enzyme activity enzyme purification fusarium oxysporum high performance liquid chromatography nonhuman ph polyacrylamide gel electrophoresis priority journal Carbohydrates Culture Media Fusarium Glycoside Hydrolases Metals Molecular Weight Fusarium oxysporum f. sp. melonis Fusarium sp. Melonis Triticum aestivum subsp. spelta Alconada, T.M. Martínez, M.J. Purification and characterization of an extracellular endo-1,4-β-xylanase from Fusarium oxysporum f. sp. melonis |
| topic_facet |
Endo-1,4-β-xylanase activity Fusarium oxysporum f. sp. melonis β-Xylosidase activity endo 1,4 beta xylanase unclassified drug xylan article enzyme activity enzyme purification fusarium oxysporum high performance liquid chromatography nonhuman ph polyacrylamide gel electrophoresis priority journal Carbohydrates Culture Media Fusarium Glycoside Hydrolases Metals Molecular Weight Fusarium oxysporum f. sp. melonis Fusarium sp. Melonis Triticum aestivum subsp. spelta |
| description |
Fusarium oxysporum f. sp. melonis produces extracellular endo-1,4-β-xylanase and β-xylosidase when grown in shaken culture at 26°C in a mineral salts medium containing oat spelt xylan and glucose as carbon sources. Endo-1,4-β-xylanase was purified 251 times from 5-day-old culture filtrates, by Sephacryl S-200, ion exchange and gel filtration HPLC. The purified sample yielded a single band in SDS polyacrylamide gels with a molecular mass of 80 kDa on electrophoretic mobility and 83 kDa by gel filtration behavior. High activity of the endo-1,4-β-xylanase against xylan was observed between 5 and 8 pH, and between 40 and 60°C, the optimum pH and temperature being 5.0 and 50°C, respectively. Kinetic properties of the enzyme are similar to those of other fungal xylanases, showing high affinity towards oat spelt xylan with a Km of 1 mM expressed as xylose equivalent. © 1994. |
| format |
JOUR |
| author |
Alconada, T.M. Martínez, M.J. |
| author_facet |
Alconada, T.M. Martínez, M.J. |
| author_sort |
Alconada, T.M. |
| title |
Purification and characterization of an extracellular endo-1,4-β-xylanase from Fusarium oxysporum f. sp. melonis |
| title_short |
Purification and characterization of an extracellular endo-1,4-β-xylanase from Fusarium oxysporum f. sp. melonis |
| title_full |
Purification and characterization of an extracellular endo-1,4-β-xylanase from Fusarium oxysporum f. sp. melonis |
| title_fullStr |
Purification and characterization of an extracellular endo-1,4-β-xylanase from Fusarium oxysporum f. sp. melonis |
| title_full_unstemmed |
Purification and characterization of an extracellular endo-1,4-β-xylanase from Fusarium oxysporum f. sp. melonis |
| title_sort |
purification and characterization of an extracellular endo-1,4-β-xylanase from fusarium oxysporum f. sp. melonis |
| url |
http://hdl.handle.net/20.500.12110/paper_03781097_v118_n3_p305_Alconada |
| work_keys_str_mv |
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