Enzymatic hydrolysis reaction of phospholipids in monolayers

Abstract The hydrolysis reaction of l- , d- and d , l -dipalmitoylphosphatidylcholine (DPPC) catalized by bee venom phospholipase A 2 was studied in spreading monolayer at the water/air interface. DPPC and the hydrolysis products, palmitic acid and l -lysophosphatidylcholine, palmitoyl were characterized at the interface by means of surface pressure, surface potential and ellipsometric measurements. Furthermore, mixed monolayers of reagents and products were investigated to ascertain their miscibility. The results show that the hydrolysis reaction can be followed by the decrease of surface pressure with time on subphases containing β-cyclodextrin, a well-known complexing agent of many amphiphilic compounds. The order of the reaction, the kinetic constant and other kinetic parameters are deduced.