Dynamic Observations of the Hydrolysis of a DPPC Monolayer at the Air/Water Interface Catalyzed by Phospholipase A2

Abstract

Three factors are important: the hydrolysis of phospholipids, in this case l-dipalmitolphosphatidylcholine (DPPC), catalyzed by phospholipase A2 is controlled through 1) enzyme penetration, 2) the cleavage reaction, and 3) the dissolution of reaction products in the subphase. The use of lipid monolayers allows these processes to be studied separately at the air/water interface. Brewster angle microscopy (BAM) is used to follow the enzyme reaction in detail; the picture shows an L-DPPC monolayer at the air/water interface after the hydrolysis reaction.