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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].
Tipo de material: Artículo en línea Artículo en línea Tema(s): Auricularia fuscosuccinea | Hongos comestibles | Fenol oxidasa | BiorremediaciónTema(s) en inglés: Auricularia fuscosuccinea | Mushrooms edible | Phenol oxidases | BioremediationNota de acceso: Acceso en línea sin restricciones En: Jacobs Journal of Enzymology and Enzyme Engineering. volumen 1, número 1 (September 2015), páginas 1-6Número de sistema: 3242Resumen:
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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.

Recurso en línea: http://jacobspublishers.com/images/Enzymology/J_J_Enzymol_Enzy_Eng_1_1_006.pdf
Lista(s) en las que aparece este ítem: José Ernesto Sánchez Vázquez
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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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