Heat stability of sheep's skim milk: Aggregation and interaction of proteins

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dc.citation.volume144
dc.contributor.authorPan Z
dc.contributor.authorYe A
dc.contributor.authorFraser K
dc.contributor.authorDave A
dc.contributor.authorSingh H
dc.date.accessioned2024-05-20T02:54:07Z
dc.date.available2024-05-20T02:54:07Z
dc.date.issued2023-09
dc.description.abstractSheep's milk proteins are susceptible to heat-induced coagulation, but the protein interactions under high heat treatment have not been determined. Heat stability and protein interactions of sheep's skim milk (SSM) at pH 6.2–7.2 were examined at 140 °C. SSM had the longest heat coagulation time at pH 6.9, but became very unstable at higher or lower pH. Protein aggregates formed consisted mainly of whey proteins and κ-casein (κ-CN)-depleted casein micelles. Modification of SSM pH alters ionic calcium concentration, dissociation of caseins and electrostatic interactions, resulting in different extents of protein interactions. The extent of dissociation of κ-CN from casein micelles increased with increasing pH (from ∼6.6 to 7.0) before and after heat treatment, contributing to κ-CN-depleted casein micelle aggregation. High ionic calcium concentrations, low levels of κ-CN on casein micelles and ready dissociation of κ-CN from casein micelles may be responsible for the low heat stability of sheep's milk.
dc.description.confidentialfalse
dc.edition.editionSeptember 2023
dc.identifier.citationPan Z, Ye A, Fraser K, Dave A, Singh H. (2023). Heat stability of sheep's skim milk: Aggregation and interaction of proteins. International Dairy Journal. 144.
dc.identifier.doi10.1016/j.idairyj.2023.105689
dc.identifier.eissn1879-0143
dc.identifier.elements-typejournal-article
dc.identifier.issn0958-6946
dc.identifier.number105689
dc.identifier.piiS0958694623001085
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/69611
dc.languageEnglish
dc.publisherElsevier Ltd
dc.publisher.urihttps://www.sciencedirect.com/science/article/pii/S0958694623001085
dc.relation.isPartOfInternational Dairy Journal
dc.rights(c) 2023 The Author/s
dc.rightsCC BY-NC-ND 4.0
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.titleHeat stability of sheep's skim milk: Aggregation and interaction of proteins
dc.typeJournal article
pubs.elements-id461793
pubs.organisational-groupOther
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