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.
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| Subjects: | Auricularia fuscosuccinea, Hongos comestibles, Fenol oxidasa, Biorremediación, |
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KOHA-OAI-ECOSUR:32422024-03-12T12:45:45ZPurification and partial characterization of a phenol oxidase from the edible mushroom Auricularia Fuscosuccinea Yanez Montalvo, Alfredo Francisco 12820 Vázquez Duhalt, Rafael autor/a 13201 Cruz López, Leopoldo Caridad Doctor autor/a 2083 Calixto Romo, María de los Ángeles Doctora autor/a 12568 Sánchez, José E. Doctor autor/a 5443 textengA 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.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.Adobe Acrobat profesional 6.0 o superiorAuricularia fuscosuccineaHongos comestiblesFenol oxidasaBiorremediaciónDisponible en líneaJacobs Journal of Enzymology and Enzyme Engineeringhttp://jacobspublishers.com/images/Enzymology/J_J_Enzymol_Enzy_Eng_1_1_006.pdfAcceso en línea sin restricciones |
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Auricularia fuscosuccinea Hongos comestibles Fenol oxidasa Biorremediación Auricularia fuscosuccinea Hongos comestibles Fenol oxidasa Biorremediación |
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Auricularia fuscosuccinea Hongos comestibles Fenol oxidasa Biorremediación Auricularia fuscosuccinea Hongos comestibles Fenol oxidasa Biorremediación Yanez Montalvo, Alfredo Francisco 12820 Vázquez Duhalt, Rafael autor/a 13201 Cruz López, Leopoldo Caridad Doctor autor/a 2083 Calixto Romo, María de los Ángeles Doctora autor/a 12568 Sánchez, José E. Doctor autor/a 5443 Purification and partial characterization of a phenol oxidase from the edible mushroom Auricularia Fuscosuccinea |
| description |
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. |
| format |
Texto |
| topic_facet |
Auricularia fuscosuccinea Hongos comestibles Fenol oxidasa Biorremediación |
| author |
Yanez Montalvo, Alfredo Francisco 12820 Vázquez Duhalt, Rafael autor/a 13201 Cruz López, Leopoldo Caridad Doctor autor/a 2083 Calixto Romo, María de los Ángeles Doctora autor/a 12568 Sánchez, José E. Doctor autor/a 5443 |
| author_facet |
Yanez Montalvo, Alfredo Francisco 12820 Vázquez Duhalt, Rafael autor/a 13201 Cruz López, Leopoldo Caridad Doctor autor/a 2083 Calixto Romo, María de los Ángeles Doctora autor/a 12568 Sánchez, José E. Doctor autor/a 5443 |
| author_sort |
Yanez Montalvo, Alfredo Francisco 12820 |
| title |
Purification and partial characterization of a phenol oxidase from the edible mushroom Auricularia Fuscosuccinea |
| title_short |
Purification and partial characterization of a phenol oxidase from the edible mushroom Auricularia Fuscosuccinea |
| title_full |
Purification and partial characterization of a phenol oxidase from the edible mushroom Auricularia Fuscosuccinea |
| title_fullStr |
Purification and partial characterization of a phenol oxidase from the edible mushroom Auricularia Fuscosuccinea |
| title_full_unstemmed |
Purification and partial characterization of a phenol oxidase from the edible mushroom Auricularia Fuscosuccinea |
| title_sort |
purification and partial characterization of a phenol oxidase from the edible mushroom auricularia fuscosuccinea |
| url |
http://jacobspublishers.com/images/Enzymology/J_J_Enzymol_Enzy_Eng_1_1_006.pdf |
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