Abstract
The dynamics of heat gelation of casein glycomacropeptide (CMP) and β-lactoglobulin (β-lg) mixtures as affected by their interactions in the aqueous phase were studied at pH 3.5 and 7.0. At pH 7.0, whereas CMP did not gel, all the mixed systems gelled, but strong synergism was observed for 25:75 CMP:β-lg ratio. In comparison, at pH 3.5 where both components gelled on their own, a strong antagonism was observed, mainly at 75:25 CMP:β-lg ratio. The behaviour of mixed gels is ascribed to the formation of electrostatically driven assembled CMP:β-lg structures, modulated by pH, which were observed by dynamic light scattering and DSC measurements.
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