Abstract
Lipase activator activated the reaction by Saccharomycopsis lipolytica lipase at neutral pH in the presence of calcium ions, and 5 μg of the activators were sufficient to cause the reaction to proceed at maximum activity in the presence of 2 μl of tributyrin and 0.4 units of the lipase in a total volume of 360μl.
To define the roles of the activator and calcium ion, we studied interactions between the activator and the lipase, between the activator and a hydrophobic interface, and between the lipase and the interface. Results suggest that the interfacial adsorption of the lipase is the limiting process of lipolysis and that it is controlled by the activator and by the concentration of calcium ions.
