Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides

Autores
Cid, Alicia Graciela; Von Ellenrieder, Guillermo Rodolfo
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
BACKGROUND: Glycosidases are often used to improve the aroma of wines via hydrolysis of glycosidic precursors. The aim of this work was to develop a method to test activity and stability of these enzymes in wine environments using p-nitrophenylglycosides, avoiding interference by colored substances. RESULTS: The proposed procedure for determination of glycosidase activity in wines involves quantification of the hydrolysis product p-nitrophenol by HPLC. The method was applied to compare the inhibition of some commercial glycosidases by red and white wines. It was found that inhibition of a β-D-glucosidase by ethanol, glucose and gluconolactone was smaller than that produced by wine. This enzyme was also inhibited by wine fractions rich in phenolic compounds and glycosides. When glycoside fractions were first hydrolyzed, their inhibition was strongly reduced. The stability of glycosidases in red wines was tested, showing a destabilizing effect of β-glucosidases that was stronger than in white wine. CONCLUSION: The method developed allows measurement of glycosidase activity on p-nitrophenylglycosides in the presence of colored wine compounds. Comparison of relative glycosidase activity in wines to that in buffer solution under the same conditions can assist in the selection of appropriate aroma-enhancing enzymes. © 2009 Society of Chemical Industry.
Fil: Cid, Alicia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; Argentina
Fil: Von Ellenrieder, Guillermo Rodolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; Argentina
Materia
Β-Glucosidase
Glycosidase Inhibition
Stability
Wine Aroma
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/61709

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spelling Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosidesCid, Alicia GracielaVon Ellenrieder, Guillermo RodolfoΒ-GlucosidaseGlycosidase InhibitionStabilityWine Aromahttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2BACKGROUND: Glycosidases are often used to improve the aroma of wines via hydrolysis of glycosidic precursors. The aim of this work was to develop a method to test activity and stability of these enzymes in wine environments using p-nitrophenylglycosides, avoiding interference by colored substances. RESULTS: The proposed procedure for determination of glycosidase activity in wines involves quantification of the hydrolysis product p-nitrophenol by HPLC. The method was applied to compare the inhibition of some commercial glycosidases by red and white wines. It was found that inhibition of a β-D-glucosidase by ethanol, glucose and gluconolactone was smaller than that produced by wine. This enzyme was also inhibited by wine fractions rich in phenolic compounds and glycosides. When glycoside fractions were first hydrolyzed, their inhibition was strongly reduced. The stability of glycosidases in red wines was tested, showing a destabilizing effect of β-glucosidases that was stronger than in white wine. CONCLUSION: The method developed allows measurement of glycosidase activity on p-nitrophenylglycosides in the presence of colored wine compounds. Comparison of relative glycosidase activity in wines to that in buffer solution under the same conditions can assist in the selection of appropriate aroma-enhancing enzymes. © 2009 Society of Chemical Industry.Fil: Cid, Alicia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; ArgentinaFil: Von Ellenrieder, Guillermo Rodolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; ArgentinaJohn Wiley & Sons Ltd2009-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/61709Cid, Alicia Graciela; Von Ellenrieder, Guillermo Rodolfo; Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides; John Wiley & Sons Ltd; Journal of the Science of Food and Agriculture; 89; 6; 4-2009; 1053-10590022-5142CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/jsfa.3554info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/jsfa.3554info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:25:13Zoai:ri.conicet.gov.ar:11336/61709instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:25:13.964CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides
title Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides
spellingShingle Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides
Cid, Alicia Graciela
Β-Glucosidase
Glycosidase Inhibition
Stability
Wine Aroma
title_short Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides
title_full Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides
title_fullStr Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides
title_full_unstemmed Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides
title_sort Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides
dc.creator.none.fl_str_mv Cid, Alicia Graciela
Von Ellenrieder, Guillermo Rodolfo
author Cid, Alicia Graciela
author_facet Cid, Alicia Graciela
Von Ellenrieder, Guillermo Rodolfo
author_role author
author2 Von Ellenrieder, Guillermo Rodolfo
author2_role author
dc.subject.none.fl_str_mv Β-Glucosidase
Glycosidase Inhibition
Stability
Wine Aroma
topic Β-Glucosidase
Glycosidase Inhibition
Stability
Wine Aroma
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv BACKGROUND: Glycosidases are often used to improve the aroma of wines via hydrolysis of glycosidic precursors. The aim of this work was to develop a method to test activity and stability of these enzymes in wine environments using p-nitrophenylglycosides, avoiding interference by colored substances. RESULTS: The proposed procedure for determination of glycosidase activity in wines involves quantification of the hydrolysis product p-nitrophenol by HPLC. The method was applied to compare the inhibition of some commercial glycosidases by red and white wines. It was found that inhibition of a β-D-glucosidase by ethanol, glucose and gluconolactone was smaller than that produced by wine. This enzyme was also inhibited by wine fractions rich in phenolic compounds and glycosides. When glycoside fractions were first hydrolyzed, their inhibition was strongly reduced. The stability of glycosidases in red wines was tested, showing a destabilizing effect of β-glucosidases that was stronger than in white wine. CONCLUSION: The method developed allows measurement of glycosidase activity on p-nitrophenylglycosides in the presence of colored wine compounds. Comparison of relative glycosidase activity in wines to that in buffer solution under the same conditions can assist in the selection of appropriate aroma-enhancing enzymes. © 2009 Society of Chemical Industry.
Fil: Cid, Alicia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; Argentina
Fil: Von Ellenrieder, Guillermo Rodolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; Argentina
description BACKGROUND: Glycosidases are often used to improve the aroma of wines via hydrolysis of glycosidic precursors. The aim of this work was to develop a method to test activity and stability of these enzymes in wine environments using p-nitrophenylglycosides, avoiding interference by colored substances. RESULTS: The proposed procedure for determination of glycosidase activity in wines involves quantification of the hydrolysis product p-nitrophenol by HPLC. The method was applied to compare the inhibition of some commercial glycosidases by red and white wines. It was found that inhibition of a β-D-glucosidase by ethanol, glucose and gluconolactone was smaller than that produced by wine. This enzyme was also inhibited by wine fractions rich in phenolic compounds and glycosides. When glycoside fractions were first hydrolyzed, their inhibition was strongly reduced. The stability of glycosidases in red wines was tested, showing a destabilizing effect of β-glucosidases that was stronger than in white wine. CONCLUSION: The method developed allows measurement of glycosidase activity on p-nitrophenylglycosides in the presence of colored wine compounds. Comparison of relative glycosidase activity in wines to that in buffer solution under the same conditions can assist in the selection of appropriate aroma-enhancing enzymes. © 2009 Society of Chemical Industry.
publishDate 2009
dc.date.none.fl_str_mv 2009-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/61709
Cid, Alicia Graciela; Von Ellenrieder, Guillermo Rodolfo; Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides; John Wiley & Sons Ltd; Journal of the Science of Food and Agriculture; 89; 6; 4-2009; 1053-1059
0022-5142
CONICET Digital
CONICET
url http://hdl.handle.net/11336/61709
identifier_str_mv Cid, Alicia Graciela; Von Ellenrieder, Guillermo Rodolfo; Inhibition and inactivation evaluation of exogenous glycosidases in wines using p-nitrophenylglycosides; John Wiley & Sons Ltd; Journal of the Science of Food and Agriculture; 89; 6; 4-2009; 1053-1059
0022-5142
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/jsfa.3554
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/jsfa.3554
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv John Wiley & Sons Ltd
publisher.none.fl_str_mv John Wiley & Sons Ltd
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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