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Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from Silybum marianum flowers

2008Journal article Open access
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dc.contributor.authorCavalli, Sandra Vairo
dc.contributor.authorSilva, Sofia V.
dc.contributor.authorCimino, Cecilia
dc.contributor.authorMalcata, F. Xavier
dc.contributor.authorPriolo, Nora
dc.date.accessioned2010-10-08T17:35:25Z
dc.date.available2010-10-08T17:35:25Z
dc.date.issued2008
dc.description.abstractThe flowers of cardoon (Asteraceae) are a rich source of aspartic peptidases which possess milk clotting activity – and are thus used in traditional cheesemaking in the Iberian Peninsula. This study was aimed at characterizing the enzymatic action of the aspartic peptidases present in flowers of Silybum marianum (L.) Gaertn. (Asteraceae), specifically upon degradation of caseins. The proteolytic activities toward Na-caseinates previously prepared from caprine and ovine milks were studied, in a comparative fashion, using urea-PAGE, tricine-SDS-PAGE, densitometry, electroblotting and sequencing. Caprine as1- and b-caseins were degraded up to 68% and 40%, respectively, during 24 h of incubation. Only one important and well-defined band corresponding to a molecular weight of 14.4 kDa – i.e. a fragment of b-casein, was observed by 12 h of hydrolysis. By 24 h of incubation, ovine as- and b-caseins were degraded up to 76% and 19%, respectively. In what concerns specificity, the major cleavage site in ovine caseinate was Leu99-Arg100 in as1-caseinpor
dc.identifier.citation"Food Chemistry". ISSN 0308-8146. 106: 3 (2008) 997–1003por
dc.identifier.urihttp://hdl.handle.net/10400.14/2741
dc.language.isoengpor
dc.publisherElsevierpor
dc.relation.publisherversionhttp://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T6R-4P6M66K-2&_user=2460358&_coverDate=02%2F01%2F2008&_alid=1490328349&_rdoc=1&_fmt=high&_orig=search&_origin=search&_zone=rslt_list_item&_cdi=5037&_sort=r&_st=13&_docanchor=&view=c&_ct=1&_acct=C000057417&_version=1&_urlVersion=0&_userid=2460358&md5=5ef7282c40ddc2dc7572eaa6eba58834&searchtype=apor
dc.subjectRennet substitutepor
dc.subjectProteolysispor
dc.subjectElectrophoresispor
dc.subjectAspartic peptidasepor
dc.subjectMilk clottingpor
dc.titleHydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from Silybum marianum flowerspor
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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