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

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dc.contributor.author Li, Meng
dc.contributor.author Auty, Mark A. E.
dc.contributor.author Crowley, Shane V.
dc.contributor.author Kelly, Alan L.
dc.contributor.author O'Mahony, James A.
dc.contributor.author Brodkorb, André
dc.date.accessioned 2018-10-23T10:21:34Z
dc.date.available 2018-10-23T10:21:34Z
dc.date.issued 2018-09-25
dc.identifier.citation Li, 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.2018.09.035 en
dc.identifier.volume 88 en
dc.identifier.startpage 190 en
dc.identifier.endpage 198 en
dc.identifier.issn 0268-005X
dc.identifier.issn 1873-7137
dc.identifier.uri http://hdl.handle.net/10468/7031
dc.identifier.doi 10.1016/j.foodhyd.2018.09.035
dc.description.abstract The 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.sponsorship Teagasc (Walsh Fellowship Scheme); Dairy Research Ireland (Irish Dairy Levy Research Trust - Project Number MDDT 6261) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Elsevier Ltd. en
dc.relation.uri http://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.uri https://creativecommons.org/licenses/by-nc-nd/4.0/ en
dc.subject Dairy proteins en
dc.subject Protein aggregation en
dc.subject β-casein en
dc.title Self-association of bovine β-casein as influenced by calcium chloride, buffer type and temperature en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Shane Crowley, Dept Of Food & Nutritional Sciences, University College Cork, Cork, Ireland. +353-21-490-3000 Email: shane.crowley@ucc.ie en
dc.internal.availability Full text available en
dc.check.info Access to this article is restricted until 12 months after publication by request of the publisher. en
dc.check.date 2019-09-25
dc.date.updated 2018-10-02T11:02:48Z
dc.description.version Accepted Version en
dc.internal.rssid 456354514
dc.contributor.funder Teagasc en
dc.contributor.funder Dairy Research Ireland
dc.description.status Peer reviewed en
dc.identifier.journaltitle Food Hydrocolloids en
dc.internal.copyrightchecked Yes en
dc.internal.licenseacceptance Yes en
dc.internal.IRISemailaddress shane.crowley@ucc.ie en


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© 2018, Elsevier Ltd. All rights reserved. This manuscript version is made available under the CC-BY-NC-ND 4.0 license. Except where otherwise noted, this item's license is described as © 2018, Elsevier Ltd. All rights reserved. This manuscript version is made available under the CC-BY-NC-ND 4.0 license.
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