In the industrialized world, dairy products constitute an important part of the diet, especially in northern Europe and North America. In these regions, milk products contribute around 30% of the total dietary protein supply and represent about 65% of the intake of animal protein. The protein content of cow’s milk ranges from 32 to 35 g/L. There are two major types of milk protein: the caseins (80%), which are represented by four distinct proteins (αs1-,αs2-, β-, and κ-caseins), and the whey proteins (20%), which are represented by proteins such as β-lactoglobulin, α-lactalbumin, and lactoferrin. These two families of proteins are opposite in terms of structure. Caseins exhibit a loose and highly flexible structure and are associated into a supramolecular structure called the micelle, whereas whey proteins have a globular, well-defined three-dimensional structure. These structural differences between the two families markedly affect the behavior of these proteins in the gastrointestinal tract and particularly their susceptibility to hydrolysis by the digestive enzymes. The nutritive value of proteins, including milk proteins, is generally associated with their capacity to provide two components: nitrogen (related to protein quantity) and essential amino acids (related to protein quality). The overall nutritional efficiency of protein is most commonly measured via nitrogen retention, which assesses protein retention. In terms of protein quality, the nutritive value is related to the amino acid composition and the bioavailability of these amino acids. The content and the bioavailability of indispensable amino acids, that is, those that cannot be synthesized in the body and consequently must be supplied through the diet, are of particular concern.