Whey protein aggregate formation during heating in the presence of κ-carrageenan

Abstract

The effect of a negatively charged polymer, κ-carrageenan, on the aggregation behaviour of whey proteins during heating was studied. Aqueous solutions of whey protein isolate (WPI) at 0.5% were heated in the presence of κ-carrageenan (0.1%) at pH 7.0. This concentration was chosen as optimal in the detection of the intermediate aggregates during chromatographic analysis. The residual unaggregated protein, the intermediate aggregates and the soluble aggregates were all examined as a function of heating time and temperature, using size-exclusion chromatography coupled with light scattering detection. The presence of κ-carrageenan did not affect the aggregation of whey proteins heated at 75 °C; however, a change in the mechanism of aggregation seemed to occur at higher temperatures, and intermediates with higher molecular mass formed at 85 °C. At 90 °C, in the presence of κ-carrageenan, the extent of WPI aggregation was much larger, as soluble aggregates were no longer present and less residual protein was recovered in the unaggregated peak.