THE EFFECTS OF AMPHIPHILIC COMPOUNDS ON T HE ACTIVITY OF PANCREATIC LIPASE IN THE DROMEDARY

The pure dromedary pancreatic lipase (DrPL) (glycerol ester hydrolase, EC 3.1.1.3) is a monomer and has a molecular mass of about 45 Kd. Thi s enzyme hydrolyses more efficiently the short than the long chains tr iacylglycerols. The lipase activity is maximal at pH range 8. DrPL is inactivated at 60 degrees C and it is not stable at pH less than 5. In this study, we show that natural detergent (NaTDC) synthetic detergen t (triton X-100) or protein BSA act as potent inhibitors of DrPL activ ity. To restore the lipase activity inhibited by NaTDC, colipase shoul d be added to the hydrolysis system. When lipase is inhibited by synth etic detergent or protein, simultaneous addition of colipase and NaTDC was required to restore the DrPL activity.