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

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dc.contributor.advisor O'Mahony, Seamus Anthony en
dc.contributor.advisor Kelly, Alan en
dc.contributor.author Gaspard, Sophie J.
dc.date.accessioned 2020-09-01T12:24:26Z
dc.date.available 2020-09-01T12:24:26Z
dc.date.issued 2019-12
dc.date.submitted 2019-12
dc.identifier.citation Gaspard, S. J. 2019. Controlling the denaturation and aggregation of whey proteins using κ-casein and caseinomacropeptide. PhD Thesis, University College Cork. en
dc.identifier.endpage 268 en
dc.identifier.uri http://hdl.handle.net/10468/10435
dc.description.abstract Whey 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.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher University College Cork en
dc.rights © 2019, Sophie J. Gaspard. en
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/4.0/ en
dc.subject Whey protein en
dc.subject Caseinomacropeptide en
dc.subject Heat stability en
dc.subject Denaturation en
dc.subject Aggregation en
dc.subject Chaperone-like activity en
dc.subject Kappa-casein en
dc.title Controlling the denaturation and aggregation of whey proteins using κ-casein and caseinomacropeptide en
dc.type Doctoral thesis en
dc.type.qualificationlevel Doctoral en
dc.type.qualificationname PhD - Doctor of Philosophy en
dc.internal.availability Full text available en
dc.description.version Accepted Version en
dc.contributor.funder Teagasc en
dc.contributor.funder Dairy Research Ireland en
dc.description.status Not peer reviewed en
dc.internal.school Food and Nutritional Sciences en
dc.internal.conferring Autumn 2020 en
dc.internal.ricu Dairy Processing Technology Centre en
dc.relation.project Teagasc (Walsh Fellowship Scheme) en
dc.relation.project Dairy Research Ireland (Dairy Levy Research Trust (project MDDT6261 “ProPart”)) en
dc.contributor.advisorexternal Brodkorb, Andre en
dc.availability.bitstream openaccess


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© 2019, Sophie J. Gaspard. Except where otherwise noted, this item's license is described as © 2019, Sophie J. Gaspard.
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