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A substrain of Bacillus cereus 569/H produced under controlled fermentation conditions in a pilot plant fermentor phospholipase‐C. A partially purified preparation showed good storage stability as a lyophylized powder and in frozen solutions. The preparation contained very small amounts of phosphomonoesterase and proteolytic activities and essentially no ribonuclease activity. The level of hemolytic activity of the preparation was much lower than that of a commercial preparation of phospholipase‐C from Clostridium. Treatment of sarcoplasmic reticulum membrane with phospholipase‐C from B. cereus and from Clostridium showed that the B. cereus enzyme caused hydrolysis of 96% of the membrane phospholipids whereas the enzyme from Clostridium could hydrolyze only 80% of the phospholipids.
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Shiloach et al. (1973) studied this question.
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