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dc.contributor.author
Lufrano, Daniela
dc.contributor.author
Faro, Rosário
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Castanheira, Pedro
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Parisi, Gustavo Daniel
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Veríssimo, Paula
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Vairo Cavalli, Sandra Elizabeth
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Simões, Isaura
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Faro, Carlos
dc.date.available
2019-04-30T19:20:43Z
dc.date.issued
2012-09
dc.identifier.citation
Lufrano, Daniela; Faro, Rosário; Castanheira, Pedro; Parisi, Gustavo Daniel; Veríssimo, Paula; et al.; Molecular cloning and characterization of procirsin, an active aspartic protease precursor from Cirsium vulgare (Asteraceae); Pergamon-Elsevier Science Ltd; Phytochemistry; 81; 9-2012; 7-18
dc.identifier.issn
0031-9422
dc.identifier.uri
http://hdl.handle.net/11336/75376
dc.description.abstract
Typical aspartic proteinases from plants of the Astereaceae family like cardosins and cyprosins are well-known milk-clotting enzymes. Their effectiveness in cheesemaking has encouraged several studies on other Astereaceae plant species for identification of new vegetable rennets. Here we report on the cloning, expression and characterization of a novel aspartic proteinase precursor from the flowers of Cirsium vulgare (Savi) Ten. The isolated cDNA encoded a protein product with 509 amino acids, termed cirsin, with the characteristic primary structure organization of plant typical aspartic proteinases. The pro form of cirsin was expressed in Escherichia coli and shown to be active without autocatalytically cleaving its pro domain. This contrasts with the acid-triggered autoactivation by pro-segment removal described for several recombinant plant typical aspartic proteinases. Recombinant procirsin displayed all typical proteolytic features of aspartic proteinases as optimum acidic pH, inhibition by pepstatin, cleavage between hydrophobic amino acids and strict dependence on two catalytic Asp residues for activity. Procirsin also displayed a high specificity towards κ-casein and milk-clotting activity, suggesting it might be an effective vegetable rennet. The findings herein described provide additional evidences for the existence of different structural arrangements among plant typical aspartic proteinases.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Pergamon-Elsevier Science Ltd
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Aspartic Proteinase
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Asteraceae
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Bull Thistle
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Cirsin
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Cirsium Vulgare
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Milk-Clotting Activity
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Pepsin-Like Protease
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Procirsin
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Molecular cloning and characterization of procirsin, an active aspartic protease precursor from Cirsium vulgare (Asteraceae)
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-04-29T14:01:20Z
dc.journal.volume
81
dc.journal.pagination
7-18
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Lufrano, Daniela. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: Faro, Rosário. Universidad de Coimbra; Portugal
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Fil: Castanheira, Pedro. Biocant; Portugal
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Fil: Parisi, Gustavo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: Veríssimo, Paula. Universidad de Coimbra; Portugal
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Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: Simões, Isaura. Universidad de Coimbra; Portugal
dc.description.fil
Fil: Faro, Carlos. Universidad de Coimbra; Portugal
dc.journal.title
Phytochemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.phytochem.2012.05.028
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0031942212002506
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