Purification and partial characterization of a phenol oxidase from the edible mushroom Auricularia fuscosuccinea
Periodo de realización: 1900/01/01 al 2015/06/01
Tipo: Artículo científico
Lugar(es) de estudio: Tapachula de Córdova y Ordoñez, Chis., México
Resumen: "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. The presence of ions (Cu2+, Na+ , Mg2+) did not improved the phenol oxidase activity. Inhibitors such as sodium sulphite, ascorbic acid and hydrazine, strongly affected the enzyme activity. This is the first report on the partial characterization a phenol oxidase produced by the fungus A. fuscosuccinea."