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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, Andre
dc.date.accessioned2021-07-26T11:29:04Z
dc.date.available2021-07-26T11:29:04Z
dc.date.issued2020-08-15
dc.identifier.citationGaspard SJ, Sharma P, Fitzgerald C, et al. Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2. Food Hydrocolloids 2020, 112, 106249 doi: https://doi.org/10.1016/j.foodhyd.2020.106249en_US
dc.identifier.issn0268-005X
dc.identifier.urihttp://hdl.handle.net/11019/2506
dc.descriptionpeer-revieweden_US
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_US
dc.description.sponsorshipDairy Levy Research Trust
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relation.ispartofseriesFood Hydrocolloids;112
dc.rights© 2020 Elsevier Ltd. All rights reserved.
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttps://www.elsevier.com/tdm/userlicense/1.0/
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectCaseinomacropeptideen_US
dc.subjectWhey proteinen_US
dc.subjectHeat stabilityen_US
dc.subjectChaperone-like activityen_US
dc.subjectGelationen_US
dc.titleInfluence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2.en_US
dc.typeArticleen_US
dc.typePreprinten_US
dc.embargo.terms2021/08/15en_US
dc.identifier.doihttps://doi.org/10.1016/j.foodhyd.2020.106249
dc.identifier.piiS0268005X2031451X
dc.contributor.sponsorDairy Research Irelanden_US
dc.contributor.sponsorTeagasc Walsh Fellowship Programmeen_US
dc.contributor.sponsorEuropean Unionen_US
dc.contributor.sponsorGrantNumberMDDT6261en_US
dc.contributor.sponsorGrantNumber2012211en_US
dc.contributor.sponsorGrantNumber713654en_US
dc.source.volume112
dc.source.beginpage106249
dc.source.journaltitleFood Hydrocolloids


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