Properties and applications of phytepsins from thistle flowers

Autores
Vairo Cavalli, Sandra Elizabeth; Lufrano, Daniela; Colombo, Maria Laura; Priolo, Nora Silvia
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Aqueous extracts of thistle flowers from the genus Cynara—Cardueae tribe Cass. (Cynareae Less.), Asteraceae Dumortier—are traditionally used in the Mediterranean region for production of artisanal cheeses. This is because of the presence of aspartic proteases (APs) with the ability to coagulate milk. Plant APs, collectively known as phytepsins (EC 3.4.23.40), are bilobed endopeptidases present in an ample variety of plant species with activity mainly at acidic pHs, and have two aspartic residues located on each side of a catalytic cleft that are responsible for catalysis. The cleavage of the scissile peptide-bond occurs primarily between residues with large hydrophobic side-chains. Even when aspartylendopeptidase activity in plants is normally present at relatively low levels overall, the flowers of several species of the Cardueae tribe possess APs with extremely high specific activities in certain tissues. For this reason, in the last two decades, APs present in thistle flowers have been the subject of intensive study. Present here is a compilation of work that summarizes the known chemical and biological properties of these proteases, as well as their biomedical and biotechnological applications.
Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lufrano, Daniela. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Colombo, Maria Laura. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Priolo, Nora Silvia. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Materia
Plant Aspartic Proteases
Thistle Flowers
Asteraceae
Phytepsins
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/23084
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Properties and applications of phytepsins from thistle flowersVairo Cavalli, Sandra ElizabethLufrano, DanielaColombo, Maria LauraPriolo, Nora SilviaPlant Aspartic ProteasesThistle FlowersAsteraceaePhytepsinshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Aqueous extracts of thistle flowers from the genus Cynara—Cardueae tribe Cass. (Cynareae Less.), Asteraceae Dumortier—are traditionally used in the Mediterranean region for production of artisanal cheeses. This is because of the presence of aspartic proteases (APs) with the ability to coagulate milk. Plant APs, collectively known as phytepsins (EC 3.4.23.40), are bilobed endopeptidases present in an ample variety of plant species with activity mainly at acidic pHs, and have two aspartic residues located on each side of a catalytic cleft that are responsible for catalysis. The cleavage of the scissile peptide-bond occurs primarily between residues with large hydrophobic side-chains. Even when aspartylendopeptidase activity in plants is normally present at relatively low levels overall, the flowers of several species of the Cardueae tribe possess APs with extremely high specific activities in certain tissues. For this reason, in the last two decades, APs present in thistle flowers have been the subject of intensive study. Present here is a compilation of work that summarizes the known chemical and biological properties of these proteases, as well as their biomedical and biotechnological applications.Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Lufrano, Daniela. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Colombo, Maria Laura. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Priolo, Nora Silvia. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaElsevier2013-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/23084Vairo Cavalli, Sandra Elizabeth; Lufrano, Daniela; Colombo, Maria Laura; Priolo, Nora Silvia; Properties and applications of phytepsins from thistle flowers; Elsevier; Phytochemistry; 92; 5-2013; 16-320031-9422CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.phytochem.2013.04.013info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0031942213001544info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:02:03Zoai:ri.conicet.gov.ar:11336/23084instacron: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:34982025-09-29 10:02:03.977CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Properties and applications of phytepsins from thistle flowers
title Properties and applications of phytepsins from thistle flowers
spellingShingle Properties and applications of phytepsins from thistle flowers
Vairo Cavalli, Sandra Elizabeth
Plant Aspartic Proteases
Thistle Flowers
Asteraceae
Phytepsins
title_short Properties and applications of phytepsins from thistle flowers
title_full Properties and applications of phytepsins from thistle flowers
title_fullStr Properties and applications of phytepsins from thistle flowers
title_full_unstemmed Properties and applications of phytepsins from thistle flowers
title_sort Properties and applications of phytepsins from thistle flowers
dc.creator.none.fl_str_mv Vairo Cavalli, Sandra Elizabeth
Lufrano, Daniela
Colombo, Maria Laura
Priolo, Nora Silvia
author Vairo Cavalli, Sandra Elizabeth
author_facet Vairo Cavalli, Sandra Elizabeth
Lufrano, Daniela
Colombo, Maria Laura
Priolo, Nora Silvia
author_role author
author2 Lufrano, Daniela
Colombo, Maria Laura
Priolo, Nora Silvia
author2_role author
author
author
dc.subject.none.fl_str_mv Plant Aspartic Proteases
Thistle Flowers
Asteraceae
Phytepsins
topic Plant Aspartic Proteases
Thistle Flowers
Asteraceae
Phytepsins
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Aqueous extracts of thistle flowers from the genus Cynara—Cardueae tribe Cass. (Cynareae Less.), Asteraceae Dumortier—are traditionally used in the Mediterranean region for production of artisanal cheeses. This is because of the presence of aspartic proteases (APs) with the ability to coagulate milk. Plant APs, collectively known as phytepsins (EC 3.4.23.40), are bilobed endopeptidases present in an ample variety of plant species with activity mainly at acidic pHs, and have two aspartic residues located on each side of a catalytic cleft that are responsible for catalysis. The cleavage of the scissile peptide-bond occurs primarily between residues with large hydrophobic side-chains. Even when aspartylendopeptidase activity in plants is normally present at relatively low levels overall, the flowers of several species of the Cardueae tribe possess APs with extremely high specific activities in certain tissues. For this reason, in the last two decades, APs present in thistle flowers have been the subject of intensive study. Present here is a compilation of work that summarizes the known chemical and biological properties of these proteases, as well as their biomedical and biotechnological applications.
Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lufrano, Daniela. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Colombo, Maria Laura. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Priolo, Nora Silvia. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
description Aqueous extracts of thistle flowers from the genus Cynara—Cardueae tribe Cass. (Cynareae Less.), Asteraceae Dumortier—are traditionally used in the Mediterranean region for production of artisanal cheeses. This is because of the presence of aspartic proteases (APs) with the ability to coagulate milk. Plant APs, collectively known as phytepsins (EC 3.4.23.40), are bilobed endopeptidases present in an ample variety of plant species with activity mainly at acidic pHs, and have two aspartic residues located on each side of a catalytic cleft that are responsible for catalysis. The cleavage of the scissile peptide-bond occurs primarily between residues with large hydrophobic side-chains. Even when aspartylendopeptidase activity in plants is normally present at relatively low levels overall, the flowers of several species of the Cardueae tribe possess APs with extremely high specific activities in certain tissues. For this reason, in the last two decades, APs present in thistle flowers have been the subject of intensive study. Present here is a compilation of work that summarizes the known chemical and biological properties of these proteases, as well as their biomedical and biotechnological applications.
publishDate 2013
dc.date.none.fl_str_mv 2013-05
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/11336/23084
Vairo Cavalli, Sandra Elizabeth; Lufrano, Daniela; Colombo, Maria Laura; Priolo, Nora Silvia; Properties and applications of phytepsins from thistle flowers; Elsevier; Phytochemistry; 92; 5-2013; 16-32
0031-9422
CONICET Digital
CONICET
url http://hdl.handle.net/11336/23084
identifier_str_mv Vairo Cavalli, Sandra Elizabeth; Lufrano, Daniela; Colombo, Maria Laura; Priolo, Nora Silvia; Properties and applications of phytepsins from thistle flowers; Elsevier; Phytochemistry; 92; 5-2013; 16-32
0031-9422
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.phytochem.2013.04.013
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0031942213001544
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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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score 13.070432

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