Purification of a phospholipase C froM Bacillus cereus

Abstract

Phospholipase C activity present in the growth medium of Bacillus cereus was purified 20-fold by chromatography on polyethyleneimine-cellulose columns, or by treatment with protamine sulfate and subsequent chromatography on DEAE-cellulose columns. Purified enzyme preparations retained the ability to hydrolyze ethanolamine phosphoglycerides in the absence of choline phosphoglycerides. A typical preparation had a specific activity of about 9 [mu]moles/min per mg toward purified diacyl glycerophosphoryl ethanolamine and a specific activity of about 15-20 [mu]moles/ min per mg toward diacyl glycerophosphorylmonomethylethanolamine and diacyl glycerophosphoryl choline. Monoacyl glycerophosphate was not hydrolyzed under similar conditions.