We present a detailed study of the evolution of the size, structure and stability of casein micelles upon acidification of skim milk typically applied in yogurt-making processes using a combination of time-resolved light and small-angle X-ray scattering experiments. While most of the available light scattering studies on casein acidification have been restricted to transparent and therefore highly diluted samples, we now profit from a newly developed multiangle 3D light scattering instrument, which allows for time-resolved measurements in highly turbid samples. Our experiments clearly demonstrate the presence of two parallel pH-dependent processes, micellar reassembly and aggregation. Using a systematic investigation of the effect of casein concentration, acidification rate, and ionic strength, we are able to decouple these two processes and obtain detailed information about the pH-induced restructuration of the casein micelle structure that occurs prior to destabilization. Moreover, our experiments also unambiguously demonstrate that these micellar reassembly processes are highly concentration dependent, and that typical light scattering studies conducted under highly diluted conditions are resulting in findings that may not be relevant for the situation encountered in industrial processes at higher concentrations. Experiments conducted with covalently cross-linked micelles, where the pH-induced reassembly has been suppressed, further confirm our findings.