Caseins form heterogeneous micelles composed of three types of disordered protein chains (alpha, beta, kappa), which include protein-bound calcium phosphate particles. We probe the stability limits of the micelle by applying hydrostatic pressure. The resulting changes of the size distribution and the average molecular weight are recorded in situ with static and dynamic light scattering. Pressure induces irreversible dissociation of the micelles into monomers above a critical value depending on their size. The critical pressure increases with temperature, pH, and calcium concentration due to the interplay of hydrophobic and electrostatic interactions. The pressure transition curves are biphasic, reflecting the equilibrium of two micelle states with different stability, average size, entropy, and calcium bound. The fast process of pressure dissociation is used to probe the slow equilibrium of the two micelle states under various conditions. Binding and release of beta-casein from the micelle is suggested as the molecular mechanism of stabilization associated with the two states. In situ FTIR spectroscopy covering the P-O stretching region indicates that bound calcium phosphate particles are released from set-vie phosphate residues at pressures above 100 MPa. The resulting imbalance of charge triggers the complete decomposition of the micelle.