Increase in the activity of Rhizopus delemar lipase on water-soluble esters by its binding with phosphatidylcholine.
Rhizopus (Rh.) delemar (ATCC 34612) C-lipase was found to exhibit a slight activity towards water-soluble esters. The hydrolytic reaction of this lipase on alpha-naphthyl acetate was competitively inhibited by the presence of olive oil or Tween 80. This finding showed that both substrates, insoluble triglyceride and water-soluble ester, were hydrolyzed at the same site on the enzyme. The activities on water-soluble esters (alpha-naphthyl acetate, beta-naphthyl acetate, methyl acetylsalicylate and Tween 80) increased on binding of lipase with phosphatidylcholine (PC), although the activity on olive oil did not change. The increase in activity on water-soluble esters was due to the increase in the Vmax for its hydrolysis. It appears that local structural change of the catalytic site on lipase occurred on binding of PC to the lipase molecule and resulted in an increase in the activity on water-soluble esters. The temperature dependence of the hydrolysis of water-soluble esters demonstrated that the activation energy was lowered on binding of PC to the lipase molecule, and this resulted in an increase in the activity.
D001665:Binding Sites; D007700:Kinetics; D008049:Lipase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010713:Phosphatidylcholines; D012233:Rhizopus / Q000201:enzymology*; D012995:Solubility; D013379:Substrate Specificity; D013696:Temperature
D010713:Phosphatidylcholines; D008049:Lipase