Kinetic study of the lipase-catalyzed synthesis of triolein

The kinetics of the synthesis of triolein catalyzed by immobilized Mucor miehei lipase were studied. Equilibrium constants for the synthesis of mono-, di-, and triolein were calculated from the equilibrium compositions for different initial ratios of glycerol and oleic acid by means of multiresponse regression. The 1,3-specific lipase can catalyze the synthesis of triolein because the ester enzymatically formed with the primary alcohol isomerizes, through acyl migration, to an ester on the secondary hydroxyl. The freed primary hydroxyl may then undergo further enzymatic conversion. The rates of isomerization depend on the concentration of oleic acid.