SUBSTRATE-INDUCED STABILITY OF THE LIPASE FROM CANDIDA-CYLINDRACEA INREVERSED MICELLES

Activity of lipase (candida cylindracea) in reversed micelles was foun d to be sustained over extended periods of time in the presence of amp hiphilic substrates. Esterification of palmitic or oleic acid and octa nol was studied to characterize the lipase activity in AOT/isooctane r eversed micelles. Complete conversion was possible even in the presenc e of stoichiometric excess of water. In the absence of acyl substrates , the enzyme lost all its activity within a few hours in reversed mice lles. Thermal effects on the enzyme activity were studied, and the enz yme stability in reversed micelles was compared to that in a bulk orga nic solvent.