Abstract In bovine milk, caseins are considered as the dominant proteins, which in total accounts for 80% of the total protein content. With balanced hydrophobic and hydrophilic amino acid chains, caseins can self-assemble into micellar forms at nanoscale and can be used as an effective carrier for delivery of hydrophobic bioactive compounds. Due to their random coil structures, caseins possess excellent stability during thermal processing, enabling their applications in food and beverages. In addition, the recent studies and understanding of the physicochemical properties of individual casein proteins have expanded their potential for other applications. This chapter reviews the physicochemical properties of caseins and casein micelles, available technologies to manipulate nanostructures of caseins, and the utilization of caseins for delivery of bioactive compounds as functional food ingredients.