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Proteolysis of ovine caseins by cardosin A, an aspartic acid proteinase from Cynara cardunculus L.

1998Artigo científico Acesso aberto
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dc.contributor.authorSilva, Sofia V.
dc.contributor.authorMalcata, F. Xavier
dc.date.accessioned2011-10-21T13:15:22Z
dc.date.available2011-10-21T13:15:22Z
dc.date.issued1998
dc.description.abstractThe breakdown of as -caseins and ~-caseins (in the form of as -caseins, the form of ~-caseins, and the form of a mixture of as- and ~-caseins in Na-caseinate) by cardosin A, one of the major two proteinases present in the flowers of Cynara cardunculus L., was experimentally studied via urea polyacrylamide gel electrophoresis. In Na-caseinate, as- and ~-caseins were degraded up to 46 and 76 %, respectively, by 10 h of hydrolysis. In separated form, as-caseins reached a leveI of degradationup to 67 %while ~-caseins were quickly and extensively degraded up to 76 %. Ingeneral, ~-caseins seemed to be more susceptible to proteolysis than as-caseins.por
dc.identifier.citationSILVA, Sofia V; MALCATA, F. Xavier - Proteolysis of ovine caseins by cardosin A, an aspartic acid proteinase from Cynara cardunculus L. . Lait. ISSN 0023-7302. Vol. 78 (1998), p. 513-519por
dc.identifier.urihttp://hdl.handle.net/10400.14/6668
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherINRA/Elsevierpor
dc.relation.publisherversionDOI: 10.1051/lait:1998548por
dc.subjectMilk proteinpor
dc.subjectEnzymepor
dc.subjectPlant rennetpor
dc.subjectElectrophoresispor
dc.titleProteolysis of ovine caseins by cardosin A, an aspartic acid proteinase from Cynara cardunculus L.por
dc.typejournal article
dspace.entity.typePublication
person.familyNameMalcata
person.givenNameFrancisco
person.identifier.ciencia-id1B13-38A5-35F5
person.identifier.orcid0000-0003-3073-1659
person.identifier.scopus-author-id7102542478
rcaap.rightsopenAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublicationa06c00da-0e2f-4434-8ede-4d7b22c0dfe9
relation.isAuthorOfPublication.latestForDiscoverya06c00da-0e2f-4434-8ede-4d7b22c0dfe9

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