The objective of this study was to investigate the influence of globular protein interfacial cross-linking on the in vitro digestibility of emulsified lipids by pancreatic lipase. 3% (wt/wt) corn oil-in-water emulsions stabilized by either lecithin or beta-lactoglobulin were prepared (pH 7). A portion of the beta-lactoglobulin stabilized emulsions was subjected to a heat treatment known to cross-link the adsorbed globular proteins (85 degrees C, 20 min). Pancreatic lipase and bile extract were then added to each emulsion at 37 degrees C (pH 7) and the evolution of the particle charge, particle size, appearance and free fatty acids released were measured over a period of 2 h. The rate and extent of lipid digestion did not differ greatly between lecithin and beta-lactoglobulin stabilized emulsions, nor did it differ greatly for unheated (BLG-U) or heated (BLG-H) beta-lactoglobulin stabilized emulsions. For example, the initial rate of lipid digestion was found to be 3.1, 3.4, and 2.3 mM fatty acids s(-1) m(-2) of lipid surface for droplets stabilized by BLG-U, BLG-H, and lecithin, respectively. Pancreatic lipase was able to adsorb to the droplet surfaces and access the emulsified lipids, regardless of the initial interfacial composition and the fact that some of the original emulsifier appeared to remain at the oil-water interface during digestion. These results help to explain why the human body is so efficient at digesting dietary triacylglycerols.