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dc.contributor.authorLoveday, SM
dc.contributor.authorYe, Aiqian
dc.contributor.authorSkelte, G. Anema
dc.contributor.authorSingh, Harjinder
dc.identifier.citationLoveday, S. M., Ye, A., Anema, S. G., & Singh, H. (2013). Heat-induced colloidal interactions of whey proteins, sodium caseinate and gum arabic in binary and ternary mixtures. Food Research International, 54(1), 111-117. doi: 10.1016/j.foodres.2013.06.013en
dc.descriptionNOTICE: this is the author’s version of a work that was accepted for publication in Food Research International. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Food Research International, 54, 1, (2013) 10.1016/j.foodres.2013.06.013en
dc.description.abstractMany food-grade proteins and polysaccharides will aggregate together when acidified or heated, due to electrostatic and hydrophobic interactions. At low concentrations, aggregates are soluble and colloidally stable, and they have potential applications as Pickering emulsifiers and nutrient carriers. Sodium caseinate (SC) and gum arabic (GA) at pH 7 will form colloidal aggregates when heated, but aggregation is largely reversed on cooling. Whey proteins (in the form of whey protein isolate, WPI) will aggregate irreversibly with GA when they are heated together, but aggregation is often so rapid and extensive that aggregates precipitate. Here we sought to overcome those limitations, and to develop an in situ method for quantifying heat-induced aggregation. Aggregation was measured using temperature controlled dynamic light scattering equipment and transmission electron microscopy. Combinations of SC, WPI and GA were heated at either pH 7 or 3.5, and the weight ratio of protein to polysaccharide was held at 1:5 for simplicity. Heat-induced colloidally stable aggregates of SC + WPI + GA did not dissociate on cooling. Aggregation was measured in situ, both in temperature ramps and with isothermal experiments. In situ measurement allowed us to avoid potential artefacts stemming from the temperature changes and measurement delays associated with ex situ measurements. This work demonstrated how the size and heat stability of colloidal protein-polysaccharide aggregates can be tailored by judicious selection of proteins, pH and heat treatment.en
dc.subjectWhey proteinen
dc.subjectGum arabicen
dc.subjectDynamic light scatteringen
dc.subjectColloidal aggregationen
dc.subjectHeat treatmenten
dc.titleHeat–induced colloidal interactions of whey proteins, sodium caseinate and gum arabic in binary and ternary mixturesen

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