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Heat-induced colloidal interactions of whey proteins, sodium caseinate and gum arabic in binary and ternary mixtures

Loveday, Simon M., Ye, Aiqian, Anema, Skelte G., Singh, Harjinder
Food research international 2013 v.54 no.1 pp. 111-117
cooling, emulsifiers, equipment, gum arabic, heat stability, heat treatment, hydrophobic bonding, light scattering, pH, sodium caseinate, temperature, transmission electron microscopy, whey protein isolate
Many 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 pH7 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 pH7 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.