Caseins are a family of phosphoproteins (αS1, αS2, β, κ) that account for nearly 80% of bovine milk proteins and that form soluble aggregates are known as "casein micelles" in which κ-casein molecules stabilize the structure. There are several models that account for the spatial conformation of casein in the micelles. One of them proposes that the micellar nucleus is formed by several submicelles, the periphery consisting of microvillosities of κ-casein Another model suggests that the nucleus is formed by casein-interlinked fibrils. Finally, the most recent model proposes a double link among the caseins for gelling to take place. All 3 models consider micelles as colloidal particles formed by casein aggregates wrapped up in soluble κ-casein molecules.
Milk-clotting proteases act on the soluble portion, κ-casein, thus originating an unstable micellar state that
results in clot formation.