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On the activity and specificity of cardosin B, a plant proteinase, on ovine caseins

dc.contributor.authorSilva, Sofia V.
dc.contributor.authorMalcata, F. Xavier
dc.date.accessioned2011-10-19T13:57:27Z
dc.date.available2011-10-19T13:57:27Z
dc.date.issued1999
dc.description.abstractThe proteolytic activity of cardosin B, an aspartic proteinase from the thistle, Cynara cardunculus, on ovine αs-caseins and β-caseins (independently or present together in sodium caseinate) was followed by urea polyacrylamide gel electrophoresis and reversed phase high performance liquid chromatography. This enzyme degraded both types of caseins, but not to the same degree. In sodium-caseinate, by 10 h at 30°C, αs-caseins were more susceptible to proteolysis by cardosin B than β-casein whereas, in isolated form, the reverse was observed. Sequencing of the peptides produced by hydrolysis of Na-caseinate showed that the major cleavage sites in αs1-casein were Leu156-Asp157 and Trp164-Tyr165 whereas, in β-casein, they were Leu127-Thr128, Leu165-Ser166 and Leu90-Tyr191. The bonds Trpl64-Tyr165 and Leu165-Ser166 were the most susceptible to cardosin B when this enzyme acted upon isolated αs1- and β-casein, respectively.por
dc.identifier.citationSILVA, Sofia V. ; MALCATA, F. Xavier - On the activity and specificity of cardosin B, a plant proteinase, on ovine caseins. Food Chemistry. ISSN 0308-8146. Vol. 67, n.º 4 (1999), p. 373-378por
dc.identifier.urihttp://hdl.handle.net/10400.14/6475
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherElsevierpor
dc.relation.publisherversiondoi:10.1016/S0308-8146(99)00126-0por
dc.subjectRennet substitutepor
dc.subjectProteolysispor
dc.subjectElectrophoresispor
dc.subjectRP-HPLCpor
dc.titleOn the activity and specificity of cardosin B, a plant proteinase, on ovine caseinspor
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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