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

• Published in: Food hydrocolloids 2021-03, Vol.112, p.106249, Article 106249
• Main Authors: Gaspard, Sophie J., Sharma, Prateek, Fitzgerald, Ciarán, Tobin, John T., O’Mahony, James A., Kelly, Alan L., Brodkorb, André
• Format: Article
• Language: English
• Subjects: Caseinomacropeptide; Chaperone-like activity; Gelation; Heat stability; Whey protein
• ISSN: 0268-005X; 1873-7137
• DOI: 10.1016/j.foodhyd.2020.106249

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