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Laboratory of Bacteriology, Department of Dairy Science, University of Illinois, Urbana
ABSTRACT
Filtrates from cultures of G. candidum contain a true lipase which was active at pH 5.0 to 8.0 over a temperature range from 20 to 37° C. Maximum activity occurred in substrate buffered at pH 6.0 and incubated at 30° C.
Naturally occurring mixed triglycerides were more readily hydrolyzed than were synthetic triglycerides and other esters. Lipolytic activity was dependent upon the type of substrate, substrate concentration, enzyme concentration and reaction time.
The lipase was inactive at pH 4.0 and was destroyed at pH 3.0. The enzyme was partially and irreversibly inactivated by oxygen. HgCl2 inhibition was partially reversed by glutathione and other reducing agents.
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