The rennet coagulation mechanism of skim milk as observed by transmission diffusing wave spectroscopy

The technique of forward-scattering diffusing wave spectroscopy has been used to study the rennet-induced gelation of skim milk. The results allow the comparison of a colloidal suspension at a realistic concentration (Φ∼10%Φ∼10%) compared with well-established measurements made on highly-diluted milk samples. It is shown that the partially renneted casein micelles do not begin to approach one another until the extent of breakdown of κ-casein has reached about 70%; above this point, they interact increasingly strongly with the extent of proteolysis. This interaction initially restricts the diffusive motion of the particles rather than causing true aggregation. Only after more extensive removal of the protective κ  -casein does true aggregation occur, with the appearance of a space-filling gel (defined by rheology as having a value of tanδ<1tanδ<1). The results show in greater detail than hitherto the progress of interactions between the particles in a system where the steric stabilization is progressively destroyed, and suggest that the renneting of milk at its normal concentration cannot be described simply by reactions between freely-diffusing particles.

Changes in light scattering (radius, l∗l∗, mean square displacement) and rheological parameters during the enzyme-induced destabilization of casein micelles.Figure optionsDownload as PowerPoint slide