Abstract
The hydrolysis of olive oil by the lipase from Chromobacterium was inhibited by the addition emulsion of organic solvents. This inhibition was essentially competitive and was observed with emulsion of any organic solvent used in this study, independently of their chemical structure. The competitive inhibition was also observed on the emulsion prepared with various emulsifiers and on the emulsion in which an organic solvent was dissolved. Lipases from porcine pancreas, Candida sp. and Pseudomonas sp. showed the same behavior. From these results, it was presumed that lipases had a characteristics of adsorption at the interface. This assumption was also supported by the experiment of adsorption to emulsions. On the other hand, the esterase of chiken liver was not inhibited by the emulsion of any organic solvents tested in this study and was not adsorbed to the emulsion. A possible hypothesis on the mechanism of lipase reaction was discussed in relation to these properties.
