Purification and partial characterization of a phenol oxidase from the edible mushroom Auricularia Fuscosuccinea
Yanez Montalvo, Alfredo Francisco
| Vázquez Duhalt, Rafael [autor/a]
| Cruz López, Leopoldo Caridad [autor/a]
| Calixto Romo, María de los Ángeles [autor/a]
| Sánchez, José E [autor/a]
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Tipo de material: ![Artículo
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Tipo de ítem | Biblioteca actual | Colección | Signatura | Estado | Fecha de vencimiento | Código de barras |
---|---|---|---|---|---|---|
Artículos | Biblioteca Electrónica Recursos en línea (RE) | ECOSUR | Recurso digital | ECO400032426408 |
Acceso en línea sin restricciones
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. eng
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