Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor
Enzyme activity and stability in a membrane reactor for wine aroma enhancement could be higher than when the enzyme is present in a free state since the catalyst would only be in contact with the low molecular weight components of this beverage. To test this hypothesis, the activity and stability of...
| Autores: | ; ; |
|---|---|
| Tipo de documento: | Artículo |
| Estado: | Published version |
| Fecha de publicación: | 2014 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Lenguaje: | Inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/7754 |
| Acceso en línea: | http://hdl.handle.net/11336/7754 |
| Nivel de acceso: | Acceso abierto |
| Palabra clave: | Glycosidases Inhibition Stability Membrane Reactor Wine Aroma https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
| _version_ | 1878402763875942400 |
|---|---|
| author | Cid, Alicia Graciela |
| author2 | Daz, Mirta Elizabeth Von Ellenrieder, Guillermo Rodolfo |
| author2_role | author author |
| author_browse | Cid, Alicia Graciela Daz, Mirta Elizabeth Von Ellenrieder, Guillermo Rodolfo |
| author_facet | Cid, Alicia Graciela Daz, Mirta Elizabeth Von Ellenrieder, Guillermo Rodolfo |
| author_role | author |
| collection | CONICET Digital (CONICET) |
| description | Enzyme activity and stability in a membrane reactor for wine aroma enhancement could be higher than when the enzyme is present in a free state since the catalyst would only be in contact with the low molecular weight components of this beverage. To test this hypothesis, the activity and stability of two commercial β-glucosidases were measured in the presence of Tannat wine and of its low molecular weight (MW) fraction (< 10 kDa) obtained by ultrafiltration. The relative activities of Endozym Rouge and Endozym β-split β-glucosidase were higher in this fraction (3.8 % and 7.6 %, respectively) than in the whole wine (0.9 % and 5.6 %, respectively). Both enzymes were also more stable in the low MW fraction. Endozym β-split β-glucosidase retained about 75 % of its initial activity after 14 days in the low MW fraction, as contrasted with only 37.5 % in the wine. The ability of Endozym Rouge β-glucosidase to hydrolyze the synthetic substrate p-nitrophenylglucoside was examined in a simple batch membrane reactor. A rate of hydrolysis comparable to that obtained with the free Endozym Rouge β-glucosidase was reached. Finally, Endozym β-split β-glucosidase was used to hydrolyze the synthetic substrate in a hollow fiber membrane reactor and a substrate conversion near 58 % was achieved. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | AR_00a0cfc6409079a9e8b8ec67969a1d5e |
| identifier_str_mv | Cid, Alicia Graciela; Daz, Mirta Elizabeth; Von Ellenrieder, Guillermo Rodolfo; Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor; University of Zagreb. Faculty of Food Technology and Biotechnology; Food Technology And Biotechnology; 52; 3; 3-2014; 334-341 1330-9862 1334-2606 |
| institution | Consejo Nacional de Investigaciones Científicas y Técnicas |
| instname_str | Consejo Nacional de Investigaciones Científicas y Técnicas |
| language | eng |
| network_acronym_str | AR |
| network_name_str | Argentina |
| oai_identifier_str | oai:ri.conicet.gov.ar:11336/7754 |
| publishDate | 2014 |
| publishDateSort | 2014 |
| publisher | University of Zagreb. Faculty of Food Technology and Biotechnology |
| publisherStr | University of Zagreb. Faculty of Food Technology and Biotechnology |
| reponame_str | CONICET Digital (CONICET) |
| spelling | Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor Cid, Alicia Graciela Daz, Mirta Elizabeth Von Ellenrieder, Guillermo Rodolfo Glycosidases Inhibition Stability Membrane Reactor Wine Aroma https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 Enzyme activity and stability in a membrane reactor for wine aroma enhancement could be higher than when the enzyme is present in a free state since the catalyst would only be in contact with the low molecular weight components of this beverage. To test this hypothesis, the activity and stability of two commercial β-glucosidases were measured in the presence of Tannat wine and of its low molecular weight (MW) fraction (< 10 kDa) obtained by ultrafiltration. The relative activities of Endozym Rouge and Endozym β-split β-glucosidase were higher in this fraction (3.8 % and 7.6 %, respectively) than in the whole wine (0.9 % and 5.6 %, respectively). Both enzymes were also more stable in the low MW fraction. Endozym β-split β-glucosidase retained about 75 % of its initial activity after 14 days in the low MW fraction, as contrasted with only 37.5 % in the wine. The ability of Endozym Rouge β-glucosidase to hydrolyze the synthetic substrate p-nitrophenylglucoside was examined in a simple batch membrane reactor. A rate of hydrolysis comparable to that obtained with the free Endozym Rouge β-glucosidase was reached. Finally, Endozym β-split β-glucosidase was used to hydrolyze the synthetic substrate in a hollow fiber membrane reactor and a substrate conversion near 58 % was achieved. Fil: Cid, Alicia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina Fil: Daz, Mirta Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina Fil: Von Ellenrieder, Guillermo Rodolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina University of Zagreb. Faculty of Food Technology and Biotechnology http://hdl.handle.net/11336/7754 Cid, Alicia Graciela; Daz, Mirta Elizabeth; Von Ellenrieder, Guillermo Rodolfo; Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor; University of Zagreb. Faculty of Food Technology and Biotechnology; Food Technology And Biotechnology; 52; 3; 3-2014; 334-341 1330-9862 1334-2606 |
| spellingShingle | Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor Cid, Alicia Graciela Glycosidases Inhibition Stability Membrane Reactor Wine Aroma https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
| status_str | publishedVersion |
| title | Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor |
| title_full | Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor |
| title_fullStr | Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor |
| title_full_unstemmed | Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor |
| title_short | Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor |
| title_sort | Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor |
| topic | Glycosidases Inhibition Stability Membrane Reactor Wine Aroma https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
| topic_facet | Glycosidases Inhibition Stability Membrane Reactor Wine Aroma https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
| url | http://hdl.handle.net/11336/7754 |