Hydrolysis of intralipid by pancreatic lipase and phospholipase A2-gel filtration studies.

Intralipid was incubated with pancreatic lipase (EC 3.1.1.3) and/or phospholipase A2 (EC 3.1.1.4) at two bile salts/phosphatidylcholine molar ratios and at two different triglyceride hydrolysis rates using various amounts of lipase. Incubations were studied by gel filtration. Results show: During lipase action, three phases of lipids coexist: an emulsified phase, a micellar phase and an intermediate heavy phase sized between the two others. The equilibrium between each phase is dependent upon the bile salts concentration. Under these conditions, pancreatic lipase was at 60% bound to the emulsified phase, whereas pancreatic phospholipase A2 was bound at 94% to the micellar phase.