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The colloidal properties of the casein micelles play a major role in the structural properties of milk protein concentrates. Because of their great technological importance, the structural-functional relationships of casein micelles have been studied for decades in skim milk; however, novel ingredients are now available with higher protein concentrations and varying in composition. The colloidal behavior of caseins in these systems is not fully understood. Concentrates prepared with membrane technologies, and subjected to pre- or post-modifications that affect their technological functionality, have become increasingly widespread. This has created large opportunities for innovation and generation of value-added ingredients. The manner in which caseins interact with themselves and the other components in these concentrates will affect the structure of the final matrix. During concentration by filtration, the interparticle distance between the micelles decreases considerably, increasing their spatial correlation and decreasing their diffusivity. Rearrangements occur due to changes in environmental conditions, such as ionic composition, osmotic stress, shear, pH, or heating temperature. This will have important consequences on bulk viscosity of the concentrates, as well as on the mode of formation of structures' building blocks. This paper aims at highlighting some of the important factors affecting the colloidal structure of casein micelles, their destabilization and network formation, namely, processing history, volume fraction, composition of the serum phase, and ionic equilibrium. Understanding these factors will lead to a better quality control of dairy ingredients and to the development of a new generation of ingredients with targeted functionality.
Corredig et al. (Thu,) studied this question.