Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2

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dc.contributor.authorGaspard, Sophie J.
dc.contributor.authorSharma, Prateek
dc.contributor.authorFitzgerald, Ciarán
dc.contributor.authorTobin, John T.
dc.contributor.authorO'Mahony, James A.
dc.contributor.authorKelly, Alan L.
dc.contributor.authorBrodkorb, André
dc.contributor.funderDairy Research Irelanden
dc.contributor.funderTeagascen
dc.contributor.funderHorizon 2020en
dc.date.accessioned2022-08-12T09:04:24Z
dc.date.available2022-08-12T09:04:24Z
dc.date.issued2021
dc.date.updated2022-08-11T15:03:52Z
dc.description.abstractThe effect of caseinomacropeptide (CMP) on the heat-induced denaturation and gelation of whey proteins (2.5-10%, w/v) at pH 6.4 and 7.2, at a whey protein:CMP ratio of 1:0.9 (w/w), was investigated using differential scanning calorimetry (DSC), oscillatory rheology (90 °C for 20 min) and confocal microscopy. Greater frequency-dependence in the presence of CMP suggested that the repulsive interactions between CMP and the whey proteins affected the network generated by the non-heated whey protein samples. At pH 6.4 or 7.2, CMP increased the temperature of denaturation of β-lactoglobulin by up to 3 °C and increased the gelation temperature by up to 7 °C. The inclusion of CMP strongly affected the structure of the heat-induced whey protein gels, resulting in a finer stranded structure at pH 6.4 and 7.2. The presence of CMP combined with a lower heating rate (2 °C/min) prevented the formation of a solid gel of whey proteins after heating for 20 min at 90 °C and at pH 7.2. These results show the potential of CMP for control of whey protein denaturation and gelation.en
dc.description.sponsorshipDairy Research Ireland (Dairy Levy Research Trust (project MDDT6261 “ProPart”)); Teagasc (Teagasc Walsh Fellowship Scheme (reference number 2012211)en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleid106249en
dc.identifier.citationGaspard, S. J., Sharma, P., Fitzgerald, C., Tobin, J. T., O'Mahony, J. A., Kelly, Alan L. and Brodkorb, A. (2021) 'Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2', Food Hydrocolloids, 112, 106249 (9pp). doi: 10.1016/j.foodhyd.2020.106249en
dc.identifier.doi10.1016/j.foodhyd.2020.106249en
dc.identifier.endpage9en
dc.identifier.issn0268-005X
dc.identifier.journaltitleFood Hydrocolloidsen
dc.identifier.startpage1en
dc.identifier.urihttps://hdl.handle.net/10468/13484
dc.identifier.volume112en
dc.language.isoenen
dc.publisherElsevieren
dc.relation.projectinfo:eu-repo/grantAgreement/EC/H2020::MSCA-COFUND-FP/713654/EU/Career Development Fellowships in the National Technology Centre Programme/Career-FITen
dc.rights© 2020, Elsevier Ltd. All rights reserved.en
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subjectCaseinomacropeptideen
dc.subjectWhey proteinen
dc.subjectHeat stabilityen
dc.subjectChaperone-like activityen
dc.subjectGelationen
dc.titleInfluence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2en
dc.typeArticle (peer-reviewed)en
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