Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2.
AuthorGaspard, Sophie J.
Tobin, John T.
O’Mahony, James A.
Kelly, Alan L.
MetadataShow full item record
StatisticsDisplay Item Statistics
CitationGaspard SJ, Sharma P, Fitzgerald C, et al. Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2. Food Hydrocolloids 2020, 112, 106249 doi: https://doi.org/10.1016/j.foodhyd.2020.106249
AbstractThe 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.
FunderDairy Research Ireland; Teagasc Walsh Fellowship Programme; European Union
Grant NumberMDDT6261; 2012211; 713654
The following license files are associated with this item:
- Creative Commons