Food proteins are the basis for imparting functionality in many foods. Not all proteins are able to form associations with other proteins, but the casein micelles present properties that make them a unique system for protein blending. This has the potential to provide novel functionalities in industrial food applications. To capitalize on this, our study investigated processing methods to stabilize the interactions of casein micelles in milk with chia protein. Most plant proteins are not soluble in water, so a co-dispersion of casein micelles with these globular proteins was sought via homogenization. First, the temperature of the skim milk was lowered, and sodium citrate was added to allow the casein micelles to dissociate enough as to interact with the chia protein. The soluble chia protein was extracted from microfine powder of the seed. The fiber, starch material, and pericarp were precipitated and separated. The supernatant containing the dispersed chia protein was added to the skim milk. This was homogenized under cold condition (4°C) and relatively higher pressure (350 bar) to increase the stability of the colloidal dispersion by applying shear. The particle size, zeta potential, and total protein were analyzed before and after homogenization. The zeta potential increased significantly after homogenization from a mean value of 33.98 to 45.83 mV. This indicates a stable co-dispersion of the chia protein and casein micelles. Overall, dissociating casein micelles and homogenizing at colder temperatures and higher pressures may effectively co-disperse and stabilize chia plant protein and casein micelles for use in a wide range of dairy applications.