Properties and applications of phytepsins from thistle flowers
- Autores
- Vairo Cavalli, Sandra Elizabeth; Lufrano, Daniela; Colombo, María Laura; Priolo de Lufrano, Nora Silvia
- Año de publicación
- 2013
- Idioma
- inglés
- Tipo de recurso
- reseña 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.
Centro de Investigación de Proteínas Vegetales - Materia
-
Biología
Plant aspartic proteases
Thistle flowers
Asteraceae
Phytepsins - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/153188
Ver los metadatos del registro completo
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Properties and applications of phytepsins from thistle flowersVairo Cavalli, Sandra ElizabethLufrano, DanielaColombo, María LauraPriolo de Lufrano, Nora SilviaBiologíaPlant aspartic proteasesThistle flowersAsteraceaePhytepsinsAqueous 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.Centro de Investigación de Proteínas Vegetales2013info:eu-repo/semantics/reviewinfo:eu-repo/semantics/publishedVersionRevisionhttp://purl.org/coar/resource_type/c_dcae04bcinfo:ar-repo/semantics/resenaArticuloapplication/pdf16-32http://sedici.unlp.edu.ar/handle/10915/153188enginfo:eu-repo/semantics/altIdentifier/issn/0031-9422info:eu-repo/semantics/altIdentifier/doi/10.1016/j.phytochem.2013.04.013info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:39:34Zoai:sedici.unlp.edu.ar:10915/153188Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:39:34.657SEDICI (UNLP) - Universidad Nacional de La Platafalse |
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 Biología 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, María Laura Priolo de Lufrano, Nora Silvia |
author |
Vairo Cavalli, Sandra Elizabeth |
author_facet |
Vairo Cavalli, Sandra Elizabeth Lufrano, Daniela Colombo, María Laura Priolo de Lufrano, Nora Silvia |
author_role |
author |
author2 |
Lufrano, Daniela Colombo, María Laura Priolo de Lufrano, Nora Silvia |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Biología Plant aspartic proteases Thistle flowers Asteraceae Phytepsins |
topic |
Biología Plant aspartic proteases Thistle flowers Asteraceae Phytepsins |
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. Centro de Investigación de Proteínas Vegetales |
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 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/review info:eu-repo/semantics/publishedVersion Revision http://purl.org/coar/resource_type/c_dcae04bc info:ar-repo/semantics/resenaArticulo |
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review |
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publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/153188 |
url |
http://sedici.unlp.edu.ar/handle/10915/153188 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/0031-9422 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.phytochem.2013.04.013 |
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info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
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openAccess |
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http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
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