Association of denatured whey proteins with casein micelles in heated reconstituted skim milk and its effect on casein micelle size.
When skim milk at pH 6.55 was heated (75 to 100 degrees C for up to 60 min), the casein micelle size, as monitored by photon correlation spectroscopy, was found to increase during the initial stages of heating and tended to plateau on prolonged heating. At any particular temperature, the casein micelle size increased with longer holding times, and, at any particular holding time, the casein micelle size increased with increasing temperature. The maximum increase in casein micelle size was about 30-35 nm. The changes in casein micelle size were poorly correlated with the level of whey protein denaturation. However, the changes in casein micelle size were highly correlated with the levels of denatured whey proteins that were associated with the casein micelles. The rate of association of the denatured whey proteins with the casein micelles was considerably slower than the rate of denaturation of the whey proteins. Removal of the whey proteins from the skim milk resulted in only small changes in casein micelle size during heating. Re-addition of beta-lactoglobulin to the whey-protein-depleted milk caused the casein micelle size to increase markedly on heat treatment. The changes in casein micelle size induced by the heat treatment of skim milk may be a consequence of the whey proteins associating with the casein micelles. However, these associated whey proteins would need to occlude a large amount of serum to account for the particle size changes. Separate experiments showed that the viscosity changes of heated milk and the estimated volume fraction changes were consistent with the particle size changes observed. Further studies are needed to determine whether the changes in size are due to the specific association of whey proteins with the micelles or whether a low level of aggregation of the casein micelles accompanies this association behaviour. Preliminary studies indicated lower levels of denatured whey proteins associated with the casein micelles and smaller changes in casein micelle size occurred as the pH of the milk was increased from pH 6.5 to pH 6.7.
Anema
Skelte G
SG
Food Science Section, Fonterra Research Centre (formerly NZDRI Ltd.), Private Bag 11029, Palmerston North, New Zealand. skelte.anema@fonterraresearch.com
Li
Yuming
Y
D000818:Animals; D002364:Caseins / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007782:Lactoglobulins / Q000008:administration & dosage; D008823:Micelles; D008892:Milk / Q000737:chemistry*; D008894:Milk Proteins / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism; D010316:Particle Size; D011489:Protein Denaturation; D014783:Viscosity; D000067816:Whey Proteins
D002364:Caseins; D007782:Lactoglobulins; D008823:Micelles; D008894:Milk Proteins; D000067816:Whey Proteins