Effect of Taurodeoxycholate, Colipase and Temperature on the Interfacial Inactivation of Porcine Pancreatic Lipase

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Abstract
Beside their inhibitory effect upon lipase adsorption, bile salts at low concentration (around 0.2 mM) enhance lipolysis slightly. This activation may be attributed to a stabilization of the adsorbed lipase brought about by low concentrations of bile salts. This hypothesis relies on several observations. For a given temperature, the activation by bile salts depends on the substrate. It is maximum for trihexanoin (trihexanoylglycerol) and does not exist for tripropionin (tripropionylglycerol). In the absence of bile salts, the optimal activities are obtained for different temperatures depending on the substrate. For a given substrate, the activation by a low concentration of bile salts depends on the temperature. It increases when the temperature is raised (up to 35-40.degree. C) and completely disappears at a sufficiently low temperature (around 10.degree. C). This temperature effect does not seem to be due to a modification of the physical parameters of the interface as measured by the interfacial tension. Colipase, like bile salts, increases the lipase activity on short-chain triglycerides but only at high temperature when lipase denaturation occurs. It has no influence upon the activity when the temperature is sufficiently low (around 10.degree. C).