Abstract
Lipase activators were extracted with ethyl ether from the culture medium of Candida paralipolytica at pH 2 and two kinds of activators were separated by silica gel column chromatography. The main component (activator A) was an oily liquid, and showed an Rf value different from that of oleic acid on thin-layer chromatograms. One mole of activator A seemed to be necessary to activate one active site of the lipase and it lowered the optimum pH of the lipase from 8.2 to 7.0. In relation to this, it was found that urea, ethanol and sodium chloride had the ability to lower the optimum pH.
