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dc.contributor.authorHavea, Palatasa
dc.contributor.authorSingh, Harjinder
dc.contributor.authorCreamer, Lawrence K
dc.date.accessioned2008-04-03T22:12:51Z
dc.date.accessioned2016-03-06T22:25:32Z
dc.date.accessioned2016-09-07T13:57:31Z
dc.date.availableNO_RESTRICTIONen_US
dc.date.available2008-04-03T22:12:51Z
dc.date.available2016-03-06T22:25:32Z
dc.date.available2016-09-07T13:57:31Z
dc.date.issued2001
dc.identifier.citationHavea, P.; Singh, H.; Creamer, L. K. (2001). Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment. Journal of Dairy Research. Vol. 68, No. 3, pp. 483-497.en_US
dc.identifier.issn0022-0299
dc.identifier.urihttp://hdl.handle.net/10179/9674
dc.description.abstractBovine b-lactoglobulin (b-lg), a-lactalbumin (a-la) and bovine serum albumin (BSA), dispersed in ultra®ltration permeate, that had been prepared from whey protein concentrate solution (100 g}kg, pH 6±8), were heated at 75 °C. The consequent protein aggregation was studied by one-dimensional (1D) and twodimensional (2D) polyacrylamide gel electrophoresis (PAGE). When 100 g b-lg}kg permeate solution was heated at 75 °C, cooled and examined, large aggregates were observed. These aggregates were partially dissociated in SDS solution to give monomers, disulphide-bonded dimers, trimers and larger aggregates. When mixtures of b-lg and a-la or BSA were heated, homopolymers of each protein as well as heteropolymers of these proteins were observed. These polymer species were also observed in a heated mixture of the three proteins. Two-dimensional PAGE of mixtures demonstrated that these polymers species contained disulphide-bonded dimers of b-lg, a-la and BSA, and 1:1 disulphide-bonded adducts of a-la and b-lg, or BSA. These results are consistent with a mechanism in which the free thiols of heattreated b-lg or BSA catalyse the formation of a range of monomers, dimers and higher polymers of a-la. It is likely that when whey protein concentrate is heated under the present conditions, BSA forms disulphide-bonded strands ahead of b-lg and that a-la aggregation with b-lg and with itself is catalysed by the heat-induced unfolded BSA and b-lg.en_US
dc.language.isoenen_US
dc.publisherCambridgeen_US
dc.relation.isformatofhttp://dx.doi.org/10.1017/S0022029901004964en_US
dc.relation.isbasedonJournal of Dairy Research. Vol. 68, No. 3, pp. 483-497.en_US
dc.subjectβ-Lactoglobulinen_US
dc.subjectα-Lactalbuminen_US
dc.subjectBovine serum albuminen_US
dc.subjectHeat-induced aggregationen_US
dc.subjectBeta-lactoglobulin
dc.subjectalpha-lactalbumin
dc.subject.otherFields of Research::290000 Engineering and Technology::290100 Industrial Biotechnology and Food Sciences::290103 Food processingen_US
dc.titleCharacterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environmenten_US
dc.typeJournal Articleen_US
dc.citation.volume68
dc.identifier.harvestedMassey_Dark
dc.identifier.harvestedMassey_Dark


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