The effects of homogenization and heat treatment on the formation and the breakdown of clots during gastric digestion of whole milk were investigated using a human gastric simulator. Homogenization and heat treatment led to formation of coagula with fragmented and crumbled structures compared with the coagulum formed from raw whole milk, but a larger fraction of the protein and more fat globules were incorporated into the coagula induced by action of the milk-clotting enzyme pepsin. The fat globules in the whole milk appeared to be embedded in the clots as they formed. After formation of the clot, the greater numbers of pores in the structures of the clots formed with homogenized milk and heated whole milk led to greater rates of protein hydrolysis by pepsin, which resulted in faster release of fat globules from the clots into the digesta. Coalescence of fat globules occurred both in the digesta and within the protein clots no matter whether they were in homogenized or heated milk samples. The formation of clots with different structures and hence the changes in the rates of protein hydrolysis and the release of milk fat into the digesta in the stomach provide important information for understanding the gastric emptying of milk and the potential to use this knowledge to manipulate the bioavailability of fat and other fat-soluble nutrients in dairy products.

This study aimed to characterize and determine the disintegration of emulsion gels in a human gastric simulator (HGS) and the physicochemical characteristics of gastric digesta. Using thermal treatment at 90 °C, whey protein emulsion gels with different structures and gel strengths were formed by varying the ionic strength. Simulated boluses of soft (containing 10 mM NaCl) and hard (200 mM NaCl) gels, which had similar particle sizes to those of human subjects, were created for gastric digestion. Soft gels disintegrated faster than hard gels in the HGS. The boluses of both gels gradually disintegrated into particles of size ∼10 μm. With further digestion, the protein matrix of the soft gel particles dissolved, the proteins were disrupted mainly by proteolysis and large quantities of oil droplets were released. In contrast, for the hard gel particles, although all proteins were hydrolysed after 240 min the breakdown of the particles was slow and no oil droplets were released after 300 min. The differences in the breakdown of soft and hard gels in the HGS were attributed to the structures of the emulsion gel, which may result in different sets of peptides in the digestion. In addition, coalescence of the oil droplets was observed only for the soft gel.

The coagulation behavior and the kinetics of protein hydrolysis of skim milk powder, milk protein concentrate (MPC), calcium-depleted MPC, sodium caseinate, whey protein isolate (WPI), and heated (90°C, 20 min) WPI under gastric conditions were examined using an advanced dynamic digestion model (i.e., a human gastric simulator). During gastric digestion, these protein ingredients exhibited various pH profiles as a function of the digestion time. Skim milk powder and MPC, which contained casein micelles, formed cohesive, ball-like curds with a dense structure after 10 min of digestion; these curds did not disintegrate over 220 min of digestion. Partly calcium-depleted MPC and sodium caseinate, which lacked an intact casein micellar structure, formed curds at approximately 40 min, and a loose, fragmented curd structure was observed after 220 min of digestion. In contrast, no curds were formed in either WPI or heated WPI after 220 min of digestion. In addition, the hydrolysis rates and the compositions of the digesta released from the human gastric simulator were different for the various protein ingredients, as detected by sodium dodecyl sulfate-PAGE. Skim milk powder and MPC exhibited slower hydrolysis rates than calcium-depleted MPC and sodium caseinate. The most rapid hydrolysis occurred in the WPI (with and without heating). This was attributed to the formation of different structured curds under gastric conditions. The results offer novel insights about the coagulation kinetics of proteins from different milk protein ingredients, highlighting the critical role of the food matrix in affecting the course of protein digestion.