Abstract
The effects of casein composition on clot formation and digestibility were investigated. Bovine α-casein formed large clots when dissolved in an acid solution, whereas the clots formed by bovine β-casein and human milk casein were extremely fine. The digestibility of bovine β-casein was superior to that of bovine α-casein upon in vitro digestion with pepsin and pancreatin under the conditions found in the infant intestinal tract. In a rat model, bovine β-casein was digested and left the stomach more rapidly. These findings suggest that the high digestibility of β-casein is due to its tendency to form fine clots.