The temperature-dependent interfacial inactivation of porcine pancreatic lipase. Effect of colipase and bile salts.
This paper confirms and extends the previous observation that colipase and bile salts stabilize pancreatic lipase against inactivation at its water/substrate interface. It is shown that colipase and bile salts above their critical micellar concentration offer better protection than either of them alone. Colipase has no effect on the catalytic efficiency of lipase against an emulsified substrate in the absence or presence of bile salts. Its reported activation of pancreatic lipolysis at high temperatures in the absence of bile salts is, most likely, fully explained by its protective effect on lipase inactivation. Colipase at high concentrations relative to lipase inhibits the enzyme activity in a competitive fashion. The temperature-dependent surface inactivation of lipase has certain consequences for the methodology of lipase activity determination.
D000818:Animals; D001647:Bile Acids and Salts / Q000494:pharmacology*; D003089:Colipases / Q000494:pharmacology*; D007700:Kinetics; D008049:Lipase / Q000037:antagonists & inhibitors*; D010179:Pancreas / Q000201:enzymology*; D011506:Proteins / Q000494:pharmacology*; D013499:Surface Properties; D013552:Swine; D013656:Taurocholic Acid / Q000494:pharmacology; D013657:Taurodeoxycholic Acid / Q000494:pharmacology; D013696:Temperature
D001647:Bile Acids and Salts; D003089:Colipases; D011506:Proteins; D013657:Taurodeoxycholic Acid; D013656:Taurocholic Acid; D008049:Lipase