Purification and characterization of a β-glucosidase from the phytopathogenic fungus Fusarium oxysporum f. sp. melonis
Fusarium oxysporum f. sp. melonis produces cellulase and β-glucosidase activities in a medium with glucose and avicel as carbon source. A β-glucosidase from this crude material was purified by gel filtration and ion exchange chromatography successively. This enzyme is a unique band of protein in SDS...
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| Autores principales: | , |
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_02668254_v22_n2_p106_Alconada |
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| Sumario: | Fusarium oxysporum f. sp. melonis produces cellulase and β-glucosidase activities in a medium with glucose and avicel as carbon source. A β-glucosidase from this crude material was purified by gel filtration and ion exchange chromatography successively. This enzyme is a unique band of protein in SDS-PAGE and isoelectric focussing. It had a molecular weight of 66,000 and a pI of 5. Using p-nitrophenyl-β-D-glucopyranoside as substrate β-glucosidase shows a K(m), of 210 μmol l -1 , an optimum pH of 5.5 and an optimum reaction temperature of 60°C, being stable in a pH range of 5-7 for 48 h at room temperature. |
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