Self-association of bovine β-casein as influenced by calcium chloride, buffer type and temperature

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dc.contributor.authorLi, Meng
dc.contributor.authorAuty, Mark A. E.
dc.contributor.authorCrowley, Shane V.
dc.contributor.authorKelly, Alan L.
dc.contributor.authorO'Mahony, James A.
dc.contributor.authorBrodkorb, André
dc.contributor.funderTeagascen
dc.contributor.funderDairy Research Ireland
dc.date.accessioned2018-10-23T10:21:34Z
dc.date.available2018-10-23T10:21:34Z
dc.date.issued2018-09-25
dc.date.updated2018-10-02T11:02:48Z
dc.description.abstractThe aim of this study was to investigate the aggregation behaviour of a pure β-casein (β-CNpure) and a β-casein concentrate (β-CNconc) as a function of temperature, buffer type (pH 6.8) and the presence of CaCl2. The particle size distribution and turbidity of β-casein (β-CN) dispersions were measured by dynamic light-scattering (DLS) and UV/vis spectroscopy between 4 and 55 °C. Upon heating (4–55 °C), the particle size of both β-CN samples increased, indicating self-association via hydrophobic interactions. It was shown that the self-association of β-CN increased with increasing β-CN concentration and that β-CNpure self-associated at significantly lower concentration than β-CNconc. Both turbidity and particle size measurements showed that the β-CN samples had similar aggregation behaviour in water and imidazole buffer (pH 6.8) but differed in sodium phosphate buffer (pH 6.8), especially at higher ionic calcium concentrations. Fourier Transform Infrared (FTIR) spectroscopy revealed very little change in the secondary structure of β-CN during heating (4–55 °C). The microstructure of β-CN aggregates was monitored during heating from 10 to 55 °C, followed by cooling to 10 °C, using polarised light microscopy. Spherical and heterogeneous aggregates were observed when heated at temperatures above 37 °C, which were reversible upon cooling. This study confirmed that β-CN undergoes self-association on heating that reverses upon cooling, with the aggregation process being highly dependent on the purity of β-CN, the solvent type and the presence of ionic calcium.en
dc.description.sponsorshipTeagasc (Walsh Fellowship Scheme); Dairy Research Ireland (Irish Dairy Levy Research Trust - Project Number MDDT 6261)en
dc.description.statusPeer revieweden
dc.description.versionAccepted Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationLi, M., Auty, M. A. E., Crowley, S. V., Kelly, A. L., O'Mahony, J. A. and Brodkorb, A. (2018) 'Self-association of bovine β-casein as influenced by calcium chloride, buffer type and temperature', Food Hydrocolloids, 88, pp. 190-198. doi:10.1016/j.foodhyd.2018.09.035en
dc.identifier.doi10.1016/j.foodhyd.2018.09.035
dc.identifier.endpage198en
dc.identifier.issn0268-005X
dc.identifier.issn1873-7137
dc.identifier.journaltitleFood Hydrocolloidsen
dc.identifier.startpage190en
dc.identifier.urihttps://hdl.handle.net/10468/7031
dc.identifier.volume88en
dc.language.isoenen
dc.publisherElsevier Ltd.en
dc.relation.urihttp://www.sciencedirect.com/science/article/pii/S0268005X18309883
dc.rights© 2018, Elsevier Ltd. All rights reserved. This manuscript version is made available under the CC-BY-NC-ND 4.0 license.en
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/en
dc.subjectDairy proteinsen
dc.subjectProtein aggregationen
dc.subjectβ-caseinen
dc.titleSelf-association of bovine β-casein as influenced by calcium chloride, buffer type and temperatureen
dc.typeArticle (peer-reviewed)en
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