Pancreatic and microbial lipases: a comparison of the interaction of pancreatic colipase with lipases of various origins.

Conjugated bile salts inhibit the the hydrolysis of triglycerides (TG) by the lipases from Rhizopus arrhizus and Geotrichum candidum. This occurs for detergent concentrations similar to those which suppress the action of mammalian pancreatic lipases upon the same substrates. However, in opposition with what is observed with the latter enzymes, the activity is not restored by the addition of pancreatic colipase. Both pancreatic and R. arrhizus lipases are inactivated at tributyrin/water interface, but only the first enzyme is protected against this surface denaturation by the pancreatic cofactor. These observations suggest that colipases synthesized in mammalian pancreas display specific interaction towards the lipases made by the same organ.