Colloidal properties of protein complexes formed in β-casein concentrate solutions as influenced by heating and cooling in the presence of different solutes

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dc.contributor.author Crowley, Shane V.
dc.contributor.author Kelly, Alan L.
dc.contributor.author O'Mahony, James A.
dc.contributor.author Lucey, John A.
dc.date.accessioned 2018-12-20T16:00:32Z
dc.date.available 2018-12-20T16:00:32Z
dc.date.issued 2018-10-28
dc.identifier.citation Crowley, S. V., Kelly, A. L., O’Mahony, J. A. and Lucey, J. A. (2019) 'Colloidal properties of protein complexes formed in β-casein concentrate solutions as influenced by heating and cooling in the presence of different solutes', Colloids and Surfaces B: Biointerfaces, 174, pp. 343-351. doi: 10.1016/j.colsurfb.2018.10.067 en
dc.identifier.volume 174 en
dc.identifier.startpage 343 en
dc.identifier.endpage 351 en
dc.identifier.issn 0927-7765
dc.identifier.uri http://hdl.handle.net/10468/7250
dc.identifier.doi 10.1016/j.colsurfb.2018.10.067
dc.description.abstract Monomeric bovine β-casein self-associates into micelles under appropriate conditions of protein concentration, serum composition and temperature. The present study investigated self-association characteristics of a β-casein concentrate (BCC) prepared from milk at pilot-scale using membrane filtration. The BCC had a casein:whey protein ratio of 77:23, with ∼95% of casein consisting of β-casein, and the remainder being mostly κ-CN. BCC was reconstituted to 1.2% protein (a typical level in infant formula) in various liquid media at pH 6.8 and incubated at different temperatures from 4 to 63 °C for 30 min. Self-association of β-casein on heating was thermo-reversible in deionised water, lactose (4, 6 or 8%) or calcium (9 mM) solutions. In most serum phases, BCC became highly opaque after incubation at 63 °C, but clarified rapidly during cooling to 25 °C. However, in simulated milk ultrafiltrate (SMUF), which has a high ionic strength and is supersaturated in calcium phosphate (CaP), BCC remained opaque during cooling to 25 °C, and retained residual turbidity after 15 h of holding at 4 °C; if SMUF was prepared without phosphate then turbidity development in BCC solutions was markedly reduced. The complexes responsible for this turbidity development were successfully dissociated with 50 mM trisodium citrate. Analysis of pH during heating and holding at 60 °C indicated that SMUF acidified continuously under the period of study, while acidification in BCC/SMUF mixtures terminated after a short period, indicating that the type of CaP formed on heating is altered in the presence of BCC. This study demonstrates that BCC ingredients exhibit pronounced temperature-dependant changes in colloidal properties that are strongly affected by the presence of minerals commonly found in nutritional product formulations. en
dc.description.sponsorship Fulbright Association (Fulbright Commission Scholarship) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Elsevier en
dc.relation.uri http://www.sciencedirect.com/science/article/pii/S0927776518307665
dc.rights © 2018 Elsevier B. V. All rights reserved. This manuscript version is made available under the CC-BY-NC-ND 4.0 license en
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/4.0/ en
dc.subject Casein en
dc.subject Micelle en
dc.subject Calcium phosphate en
dc.subject Self-association en
dc.subject Turbidity en
dc.subject Precipitation en
dc.subject Sedimentation en
dc.subject Protein-mineral interactions en
dc.title Colloidal properties of protein complexes formed in β-casein concentrate solutions as influenced by heating and cooling in the presence of different solutes 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 item is restricted until 24 months after publication by request of the publisher. en
dc.check.date 2010-10-28
dc.date.updated 2018-12-20T15:48:34Z
dc.description.version Accepted Version en
dc.internal.rssid 459096042
dc.contributor.funder Fulbright Association en
dc.contributor.funder Food Institutional Research Measure en
dc.contributor.funder Department of Agriculture, Food and the Marine en
dc.description.status Peer reviewed en
dc.identifier.journaltitle Colloids and Surfaces B-Biointerfaces en
dc.internal.copyrightchecked No !!CORA!! en
dc.internal.licenseacceptance Yes en
dc.internal.IRISemailaddress shane.crowley@ucc.ie en


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© 2018 Elsevier B. V. 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 B. V. All rights reserved. This manuscript version is made available under the CC-BY-NC-ND 4.0 license
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