Controlling the denaturation and aggregation of whey proteins using κ-casein and caseinomacropeptide

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dc.availability.bitstreamopenaccess
dc.contributor.advisorO'Mahony, Seamus Anthonyen
dc.contributor.advisorKelly, Alanen
dc.contributor.advisorexternalBrodkorb, Andreen
dc.contributor.authorGaspard, Sophie J.
dc.contributor.funderTeagascen
dc.contributor.funderDairy Research Irelanden
dc.date.accessioned2020-09-01T12:24:26Z
dc.date.available2020-09-01T12:24:26Z
dc.date.issued2019-12
dc.date.submitted2019-12
dc.description.abstractWhey proteins ingredients are extensively used in a variety of product formulations such as dairy beverages, infant formula and sport nutritional beverages, due to their nutritional and functional properties. Dairy protein-containing beverages are thermally processed, typically to ensure microbiological safety. However, whey proteins denature and aggregate at temperatures greater than 60°C, which can lead to fouling of industrial equipment and/or uncontrolled gelation, depending on formulation and heating conditions. The presence of caseins has been previously reported to limit the extent of aggregation of whey proteins. The objective of this study was to investigate the effect of κ-casein and caseinomacropeptide (CMP) on the denaturation and aggregation of whey proteins, with a view to developing practical strategies for controlling whey protein denaturation and aggregation for ingredient applications. This study demonstrated that both κ-casein and CMP have the ability to improve the heat stability of whey proteins. The inclusion of κ-casein reduced the size of the aggregates of whey protein after a first heat treatment (90°C for 25 min at pH 7.2) and enhanced their solubility during subsequent heating (90°C for 1 h at pH 7.2). The presence of CMP during heating increased the temperatures of denaturation and gelation of whey proteins and prevented the formation of solid whey protein gels when combined with a low heating rate. The presence of CMP also resulted in a lower turbidity of whey protein solutions after heating and an enhanced solubility of whey protein aggregates. The effect of glycosylation of CMP on the denaturation and aggregation of whey proteins was pH-dependent; a transition occurred at pH 6, below which the glycosylation of CMP reduced its stabilizing properties. This thesis provides new insights into the interactions of whey proteins with κ-casein and CMP, with potential for novel applications in improving the heat-stability and solubility of whey proteins. The outcomes of this study have applications for the manufacture of clear, heat-stable beverages containing whey proteins.en
dc.description.statusNot peer revieweden
dc.description.versionAccepted Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationGaspard, S. J. 2019. Controlling the denaturation and aggregation of whey proteins using κ-casein and caseinomacropeptide. PhD Thesis, University College Cork.en
dc.identifier.endpage268en
dc.identifier.urihttps://hdl.handle.net/10468/10435
dc.language.isoenen
dc.publisherUniversity College Corken
dc.relation.projectTeagasc (Walsh Fellowship Scheme)en
dc.relation.projectDairy Research Ireland (Dairy Levy Research Trust (project MDDT6261 “ProPart”))en
dc.rights© 2019, Sophie J. Gaspard.en
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/en
dc.subjectWhey proteinen
dc.subjectCaseinomacropeptideen
dc.subjectHeat stabilityen
dc.subjectDenaturationen
dc.subjectAggregationen
dc.subjectChaperone-like activityen
dc.subjectKappa-caseinen
dc.titleControlling the denaturation and aggregation of whey proteins using κ-casein and caseinomacropeptideen
dc.typeDoctoral thesisen
dc.type.qualificationlevelDoctoralen
dc.type.qualificationnamePhD - Doctor of Philosophyen
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