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Quantitative studies on the enzymatic hydrolysis of milk proteins brought about by cardosins precipitated by ammonium sulfate

2001Journal article Open access
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dc.contributor.authorBarros, Rui M.
dc.contributor.authorFerreira, Carla A. Ferreira
dc.contributor.authorSilva, Sofia V. Silva
dc.contributor.authorMalcata, F. Xavier
dc.date.accessioned2011-10-22T17:07:59Z
dc.date.available2011-10-22T17:07:59Z
dc.date.issued2001
dc.description.abstractHydrolysis of whey proteins may produce peptide mixtures with better functional properties than the original protein mixture, viz. higher solubilites and lower allergenic effects. Cynara cardunculus is a wild plant that possesses (aspartic) proteases in its flower cells; those enzymes exhibit general proteolytic and specific milk clotting activities, which are rather useful in traditional cheesemaking. This study was thus aimed at characterizing the enzymatic action of crude extracts of said plant after preliminary purification by salting out with ammonium sulfate at two different concentration levels, viz. 30% and 70% saturation. The coagulant activity on milk, and the proteolytic activity using casein and azocasein as substrates, of the crude extract and of each precipitated fraction were measured at 37°C and pH 5.2. The profile of hydrolysis of the major whey proteins, i.e. α-lactalbumin (α-La), β-lactoglobulin (β-Lg) and bovine serum albumin (BSA) was characterized by gel permeation chromatography and polyacrylamide gel electrophoresis (PAGE) in the presence of sodium dodecyl sulfate. The 30% and 70% saturation fractions exhibited lower coagulant and proteolytic specific activities than the crude extract. However, the relative ratio of coagulant to proteolytic activity, which is a useful indicator of appropriateness for cheesemaking, was higher for the partially purified fractions. The extents of hydrolysis of whey proteins brought about by the partially purified extracts were above those by their crude counterpart, but qualitative hydrolysis patterns were essentially identical to each other; by 24 h, α-La was substantially depleted, whereas β-Lg was very poorly hydrolyzed and BSA was only slightly hydrolyzed. The native proteins were converted to lower and lower molecular weight peptides.por
dc.identifier.citationBARROS, M...[et al.] - Quantitative studies on the enzymatic hydrolysis of milk proteins brought about by cardosins precipitated by ammonium sulfate.Enzyme and Microbial Technology. ISSN 0141-0229. Vol. 29, n.º 8-9 (2001) p. 541-547por
dc.identifier.doi10.1016/S0141-0229(01)00431-8
dc.identifier.urihttp://hdl.handle.net/10400.14/6856
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherElsevierpor
dc.relation.publisherversiondoi:10.1016/S0141-0229(01)00431-8por
dc.subjectDairy foodspor
dc.subjectPlant rennetpor
dc.subjectProteasespor
dc.subjectWhey proteinspor
dc.titleQuantitative studies on the enzymatic hydrolysis of milk proteins brought about by cardosins precipitated by ammonium sulfatepor
dc.typejournal article
dspace.entity.typePublication
person.familyNameBARROS
person.familyNameMalcata
person.givenNameRUI
person.givenNameFrancisco
person.identifier.ciencia-id111D-8A7B-0ED1
person.identifier.ciencia-id1B13-38A5-35F5
person.identifier.orcid0000-0001-5123-2918
person.identifier.orcid0000-0003-3073-1659
person.identifier.ridJ-3340-2015
person.identifier.scopus-author-id7102542478
rcaap.rightsopenAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublicationa7bdc538-6d0d-4096-9998-a7be5d07e5d6
relation.isAuthorOfPublicationa06c00da-0e2f-4434-8ede-4d7b22c0dfe9
relation.isAuthorOfPublication.latestForDiscoverya06c00da-0e2f-4434-8ede-4d7b22c0dfe9

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