Skim milk was heated at 85-degrees-C for different holding times. As a
result of such heating, whey proteins, in particular beta-lactoglobul
in, denatured and associated with casein micelles. This led to an incr
ease in size of the casein micelles but also to a different interactio
n between them. Both these changes could be described by using a quant
itative model which was developed for the viscosity of so-called adhes
ive hard spheres. We applied the model successfully to skim milk and w
ere able to describe on a quantitative basis the changes due to the he
at treatment of milk. It was shown that after heating the casein micel
les became larger and acquired a mutual attraction. The unfolding of t
he whey proteins and their subsequent association with the casein mice
lles appeared to be responsible for these changes. How this reaction i
nfluences the fouling of heat exchangers is discussed.