Sequential hydrolysis of three acyl ester bonds in triolein molecule by human gastric juice lipase.

Specificity of gastric juice lipase concerning the sequential hydrolysis of three acyl ester bonds of triolein molecule has been compared with that of pancreatic lipase. The rates of the individual hydrolytic steps were calculated by applying the method based on the amounts of chromatographically separated hydrolysis products present upon the incubation of tritium-labelled triolein with a lipolytic enzyme. It was found that in the case of gastric lipase the rates of all three steps of triolein hydrolysis are similar, whereas in the case of pancreatic lipase the last step proceeds at a much slower rate than the preceding ones.