Purification and partial characterization of a phenol oxidase from the edible mushroom Auricularia Fuscosuccinea
A phenol oxidase from Auricularia fuscosuccinea was purified and partially characterized. Extracellular enzyme phenol oxidase was purified up to 55.9-fold from the culture filtrate by a protocol of three steps, ammonium sulfate precipitation twice (50 and 80% w/v), then two columns of ion exchange chromatography, first a DEAE-cellulose column and finally a high affinity resin column. The purified enzyme showed a molecular mass of 100 kDa, a kcat value of 2410 (±160) min-1 and KM of 240 (± 30) mM when catechol is used as substrate. The enzyme showed a maximal activity of pH and temperature at 6.0 and to 40°C, respectively. The presence of ions (Cu2+, Na+, Mg2+) did not improve the phenol oxidase activity. Inhibitors such as ascorbic acid and hydrazine, strongly affected the enzymatic activity. This is the first report on the partial characterization a phenol oxidase produced by the fungus A. fuscosuccinea.
| Main Authors: | , , , , |
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| Format: | Texto biblioteca |
| Language: | eng |
| Subjects: | Auricularia fuscosuccinea, Hongos comestibles, Fenol oxidasa, Biorremediación, |
| Online Access: | http://jacobspublishers.com/images/Enzymology/J_J_Enzymol_Enzy_Eng_1_1_006.pdf |
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