<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-09-24T06:15:44Z</responseDate><request verb="GetRecord" identifier="oai:cora.ucc.ie:10468/10435" metadataPrefix="dim">https://cora.ucc.ie/server/oai/request</request><GetRecord><record><header><identifier>oai:cora.ucc.ie:10468/10435</identifier><datestamp>2023-04-04T10:41:35Z</datestamp><setSpec>com_10468_388</setSpec><setSpec>com_10468_5</setSpec><setSpec>com_10468_9966</setSpec><setSpec>com_10468_6</setSpec><setSpec>com_10468_74</setSpec><setSpec>com_10468_1</setSpec><setSpec>col_10468_389</setSpec><setSpec>col_10468_10431</setSpec><setSpec>col_10468_458</setSpec><setSpec>col_10468_8983</setSpec></header><metadata><dim:dim xmlns:dim="http://www.dspace.org/xmlns/dspace/dim" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.dspace.org/xmlns/dspace/dim http://www.dspace.org/schema/dim.xsd">
   <dim:field mdschema="dc" element="availability" qualifier="bitstream">openaccess</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="advisor" lang="en">O&amp;apos;Mahony, Seamus Anthony</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="advisor" lang="en">Kelly, Alan</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="advisorexternal" lang="en">Brodkorb, Andre</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author">Gaspard, Sophie J.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="funder" lang="en" authority="a577cdda47dd17a9b772508710d51e0f991ca47f" confidence="600">Teagasc</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="funder" lang="en">Dairy Research Ireland</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="accessioned">2020-09-01T12:24:26Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="available">2020-09-01T12:24:26Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued">2019-12</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="submitted">2019-12</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en">Whey proteins ingredients are extensively used in a variety of product formulations &#xd;
such as dairy beverages, infant formula and sport nutritional beverages, due to their &#xd;
nutritional and functional properties. Dairy protein-containing beverages are &#xd;
thermally processed, typically to ensure microbiological safety. However, whey &#xd;
proteins denature and aggregate at temperatures greater than 60°C, which can lead to &#xd;
fouling of industrial equipment and/or uncontrolled gelation, depending on &#xd;
formulation and heating conditions. The presence of caseins has been previously &#xd;
reported to limit the extent of aggregation of whey proteins. The objective of this &#xd;
study was to investigate the effect of κ-casein and caseinomacropeptide (CMP) on &#xd;
the denaturation and aggregation of whey proteins, with a view to developing &#xd;
practical strategies for controlling whey protein denaturation and aggregation for &#xd;
ingredient applications. This study demonstrated that both κ-casein and CMP have &#xd;
the ability to improve the heat stability of whey proteins. The inclusion of κ-casein &#xd;
reduced the size of the aggregates of whey protein after a first heat treatment (90°C &#xd;
for 25 min at pH 7.2) and enhanced their solubility during subsequent heating (90°C &#xd;
for 1 h at pH 7.2). The presence of CMP during heating increased the temperatures &#xd;
of denaturation and gelation of whey proteins and prevented the formation of solid &#xd;
whey protein gels when combined with a low heating rate. The presence of CMP &#xd;
also resulted in a lower turbidity of whey protein solutions after heating and an &#xd;
enhanced solubility of whey protein aggregates. The effect of glycosylation of CMP &#xd;
on the denaturation and aggregation of whey proteins was pH-dependent; a transition &#xd;
occurred at pH 6, below which the glycosylation of CMP reduced its stabilizing &#xd;
properties. This thesis provides new insights into the interactions of whey proteins &#xd;
with κ-casein and CMP, with potential for novel applications in improving the &#xd;
heat-stability and solubility of whey proteins. The outcomes of this study have &#xd;
applications for the manufacture of clear, heat-stable beverages containing whey &#xd;
proteins.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="status" lang="en">Not peer reviewed</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="version" lang="en">Accepted Version</dim:field>
   <dim:field mdschema="dc" element="format" qualifier="mimetype" lang="en">application/pdf</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="citation" lang="en">Gaspard, S. J. 2019. Controlling the denaturation and aggregation of whey proteins using κ-casein and caseinomacropeptide. PhD Thesis, University College Cork.</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="endpage" lang="en">268</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">https://hdl.handle.net/10468/10435</dim:field>
   <dim:field mdschema="dc" element="language" qualifier="iso" lang="en">en</dim:field>
   <dim:field mdschema="dc" element="publisher" lang="en">University College Cork</dim:field>
   <dim:field mdschema="dc" element="relation" qualifier="project" lang="en">Teagasc (Walsh Fellowship Scheme)</dim:field>
   <dim:field mdschema="dc" element="relation" qualifier="project" lang="en">Dairy Research Ireland (Dairy Levy Research Trust (project MDDT6261 “ProPart”))</dim:field>
   <dim:field mdschema="dc" element="rights" lang="en">© 2019, Sophie J. Gaspard.</dim:field>
   <dim:field mdschema="dc" element="rights" qualifier="uri" lang="en">https://creativecommons.org/licenses/by-nc-nd/4.0/</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en">Whey protein</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en">Caseinomacropeptide</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en">Heat stability</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en">Denaturation</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en">Aggregation</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en">Chaperone-like activity</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en">Kappa-casein</dim:field>
   <dim:field mdschema="dc" element="title" lang="en">Controlling the denaturation and aggregation of whey proteins using κ-casein and caseinomacropeptide</dim:field>
   <dim:field mdschema="dc" element="type" lang="en">Doctoral thesis</dim:field>
   <dim:field mdschema="dc" element="type" qualifier="qualificationlevel" lang="en">Doctoral</dim:field>
   <dim:field mdschema="dc" element="type" qualifier="qualificationname" lang="en">PhD - Doctor of Philosophy</dim:field>info:eu-repo/semantics/openAccess</dim:dim></metadata></record></GetRecord></OAI-PMH>