The dissociation of the natural casein micelles in suspension containing chelating salts was studied using static and dynamic light scattering. The formation of so-called submicelles with a molar mass of about 200kgmol−1 and a hydrodynamic radius of about 12nm was observed. Heat-induced aggregation and gelation of casein submicelles in polyphosphate was studied using in situ light scattering measurements. Aggregation occurred after an induction time and involves weak interactions with apparent activation energy of about 40kJmol−1. A systematic study was made of the effect of casein concentration, temperature and pH. The aggregation rate increased with increasing temperature or casein concentration. The stability of casein submicelles in polyphosphate was maximal at pHmg align=center border=0 SRC=/images/glyphs/BQ4.GIF>6. The structure of the gels depended strongly on the casein concentration and the pH.