Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers
- Autores
- Vairo Cavalli, Sandra Elizabeth; Silva, Sofía V.; Cimino, Cecilia Verónica; Malcata, F. Xavier; Priolo de Lufrano, Nora Silvia
- Año de publicación
- 2008
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The flowers of cardoon (Asteraceae) are a rich source of aspartic peptidases which possess milk clotting activity – and are thus used in traditional cheesemaking in the Iberian Peninsula. This study was aimed at characterizing the enzymatic action of the aspartic peptidases present in flowers of Silybum marianum (L.) Gaertn. (Asteraceae), specifically upon degradation of caseins. The proteolytic activities toward Na-caseinates previously prepared from caprine and ovine milks were studied, in a comparative fashion, using urea-PAGE, tricine-SDS-PAGE, densitometry, electroblotting and sequencing. Caprine αs1- and β-caseins were degraded up to 68% and 40%, respectively, during 24 h of incubation. Only one important and well-defined band corresponding to a molecular weight of 14.4 kDa – i.e. a fragment of β-casein, was observed by 12 h of hydrolysis. By 24 h of incubation, ovine αs- and β-caseins were degraded up to 76% and 19%, respectively. In what concerns specificity, the major cleavage site in ovine caseinate was Leu99-Arg100 in αs1-casein.
Centro de Investigación de Proteínas Vegetales - Materia
-
Biología
Rennet substitute
Proteolysis
Electrophoresis
Aspartic peptidase
Milk clotting - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/128229
Ver los metadatos del registro completo
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Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowersVairo Cavalli, Sandra ElizabethSilva, Sofía V.Cimino, Cecilia VerónicaMalcata, F. XavierPriolo de Lufrano, Nora SilviaBiologíaRennet substituteProteolysisElectrophoresisAspartic peptidaseMilk clottingThe flowers of cardoon (Asteraceae) are a rich source of aspartic peptidases which possess milk clotting activity – and are thus used in traditional cheesemaking in the Iberian Peninsula. This study was aimed at characterizing the enzymatic action of the aspartic peptidases present in flowers of Silybum marianum (L.) Gaertn. (Asteraceae), specifically upon degradation of caseins. The proteolytic activities toward Na-caseinates previously prepared from caprine and ovine milks were studied, in a comparative fashion, using urea-PAGE, tricine-SDS-PAGE, densitometry, electroblotting and sequencing. Caprine αs1- and β-caseins were degraded up to 68% and 40%, respectively, during 24 h of incubation. Only one important and well-defined band corresponding to a molecular weight of 14.4 kDa – i.e. a fragment of β-casein, was observed by 12 h of hydrolysis. By 24 h of incubation, ovine αs- and β-caseins were degraded up to 76% and 19%, respectively. In what concerns specificity, the major cleavage site in ovine caseinate was Leu99-Arg100 in αs1-casein.Centro de Investigación de Proteínas Vegetales2008info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf997-1003http://sedici.unlp.edu.ar/handle/10915/128229enginfo:eu-repo/semantics/altIdentifier/issn/0308-8146info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodchem.2007.07.015info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:30:58Zoai:sedici.unlp.edu.ar:10915/128229Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:30:59.091SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers |
title |
Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers |
spellingShingle |
Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers Vairo Cavalli, Sandra Elizabeth Biología Rennet substitute Proteolysis Electrophoresis Aspartic peptidase Milk clotting |
title_short |
Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers |
title_full |
Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers |
title_fullStr |
Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers |
title_full_unstemmed |
Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers |
title_sort |
Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers |
dc.creator.none.fl_str_mv |
Vairo Cavalli, Sandra Elizabeth Silva, Sofía V. Cimino, Cecilia Verónica Malcata, F. Xavier Priolo de Lufrano, Nora Silvia |
author |
Vairo Cavalli, Sandra Elizabeth |
author_facet |
Vairo Cavalli, Sandra Elizabeth Silva, Sofía V. Cimino, Cecilia Verónica Malcata, F. Xavier Priolo de Lufrano, Nora Silvia |
author_role |
author |
author2 |
Silva, Sofía V. Cimino, Cecilia Verónica Malcata, F. Xavier Priolo de Lufrano, Nora Silvia |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Biología Rennet substitute Proteolysis Electrophoresis Aspartic peptidase Milk clotting |
topic |
Biología Rennet substitute Proteolysis Electrophoresis Aspartic peptidase Milk clotting |
dc.description.none.fl_txt_mv |
The flowers of cardoon (Asteraceae) are a rich source of aspartic peptidases which possess milk clotting activity – and are thus used in traditional cheesemaking in the Iberian Peninsula. This study was aimed at characterizing the enzymatic action of the aspartic peptidases present in flowers of Silybum marianum (L.) Gaertn. (Asteraceae), specifically upon degradation of caseins. The proteolytic activities toward Na-caseinates previously prepared from caprine and ovine milks were studied, in a comparative fashion, using urea-PAGE, tricine-SDS-PAGE, densitometry, electroblotting and sequencing. Caprine αs1- and β-caseins were degraded up to 68% and 40%, respectively, during 24 h of incubation. Only one important and well-defined band corresponding to a molecular weight of 14.4 kDa – i.e. a fragment of β-casein, was observed by 12 h of hydrolysis. By 24 h of incubation, ovine αs- and β-caseins were degraded up to 76% and 19%, respectively. In what concerns specificity, the major cleavage site in ovine caseinate was Leu99-Arg100 in αs1-casein. Centro de Investigación de Proteínas Vegetales |
description |
The flowers of cardoon (Asteraceae) are a rich source of aspartic peptidases which possess milk clotting activity – and are thus used in traditional cheesemaking in the Iberian Peninsula. This study was aimed at characterizing the enzymatic action of the aspartic peptidases present in flowers of Silybum marianum (L.) Gaertn. (Asteraceae), specifically upon degradation of caseins. The proteolytic activities toward Na-caseinates previously prepared from caprine and ovine milks were studied, in a comparative fashion, using urea-PAGE, tricine-SDS-PAGE, densitometry, electroblotting and sequencing. Caprine αs1- and β-caseins were degraded up to 68% and 40%, respectively, during 24 h of incubation. Only one important and well-defined band corresponding to a molecular weight of 14.4 kDa – i.e. a fragment of β-casein, was observed by 12 h of hydrolysis. By 24 h of incubation, ovine αs- and β-caseins were degraded up to 76% and 19%, respectively. In what concerns specificity, the major cleavage site in ovine caseinate was Leu99-Arg100 in αs1-casein. |
publishDate |
2008 |
dc.date.none.fl_str_mv |
2008 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo 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://sedici.unlp.edu.ar/handle/10915/128229 |
url |
http://sedici.unlp.edu.ar/handle/10915/128229 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/0308-8146 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodchem.2007.07.015 |
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info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
dc.format.none.fl_str_mv |
application/pdf 997-1003 |
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