Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2.

Abstract The effect of caseinomacropeptide (CMP) on the heat-induced denaturation and gelation whey proteins (2.5–10%, w/v) at pH 6.4 7.2, a protein:CMP ratio 1:0.9 (w/w), was investigated using differential scanning calorimetry (DSC), oscillatory rheology (90 °C for 20 min) confocal microscopy. Greater frequency-dependence in presence CMP suggested that repulsive interactions between affected network generated by non-heated protein samples. At or increased temperature β-lactoglobulin up to 3 °C 7 °C. inclusion strongly structure gels, resulting finer stranded 7.2. combined with lower heating rate (2 °C/min) prevented formation solid gel after 20 min at 90 °C These results show potential control gelation.