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dc.date.accessioned 2023-05-18T15:15:04Z
dc.date.available 2023-05-18T15:15:04Z
dc.date.issued 2013
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/153188
dc.description.abstract 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. es
dc.format.extent 16-32 es
dc.language en es
dc.subject Plant aspartic proteases es
dc.subject Thistle flowers es
dc.subject Asteraceae es
dc.subject Phytepsins es
dc.title Properties and applications of phytepsins from thistle flowers en
dc.type Articulo es
sedici.identifier.other https://doi.org/10.1016/j.phytochem.2013.04.013 es
sedici.identifier.issn 0031-9422 es
sedici.creator.person Vairo Cavalli, Sandra Elizabeth es
sedici.creator.person Lufrano, Daniela es
sedici.creator.person Colombo, María Laura es
sedici.creator.person Priolo de Lufrano, Nora Silvia es
sedici.subject.materias Biología es
sedici.description.fulltext true es
mods.originInfo.place Centro de Investigación de Proteínas Vegetales es
sedici.subtype Revision es
sedici.rights.license Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by-nc-sa/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle Phytochemistry es
sedici.relation.journalVolumeAndIssue vol. 92 es


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Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) Excepto donde se diga explícitamente, este item se publica bajo la siguiente licencia Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)