Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2
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Published Version
Date
2021
Authors
Gaspard, Sophie J.
Sharma, Prateek
Fitzgerald, Ciarán
Tobin, John T.
O'Mahony, James A.
Kelly, Alan L.
Brodkorb, André
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier
Published Version
Abstract
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.
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Keywords
Caseinomacropeptide , Whey protein , Heat stability , Chaperone-like activity , Gelation
Citation
Gaspard, S. J., Sharma, P., Fitzgerald, C., Tobin, J. T., O'Mahony, J. A., Kelly, Alan L. and Brodkorb, A. (2021) 'Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2', Food Hydrocolloids, 112, 106249 (9pp). doi: 10.1016/j.foodhyd.2020.106249