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
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/128229

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network_name_str SEDICI (UNLP)
spelling 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
dc.rights.none.fl_str_mv 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
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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