Abstract
The hydrolysis of soybean phospholipid comprised of phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylinositol (PI) and phosphatidic acid (PA) by a phospholipase C from Bacillus sp. was studied under various conditions.
Phospholipase C hydrolyzed preferentially PC, followed by PE>PI>PA in a biphasic reaction system of diethyl ether-phosphate buffer, while in aqueous systems, it hydrolyzed preferentially PI, followed by PC>PE> PA.
PC and PE was hydrolyzed more easily in an aqueous system with phosphate buffer at pH 7.0 than with Tris-HCl buffer at pH 7.5, while the hydrolysis of PI showed a little difference between the two buffers. PA was the most difficult to be hydrolyzed in the phospholipid mixture used.
The hydrolysis in the biphasic system of diethylether-phosphate buffer by phospholipase C from Bacillus sp. would appear to be a simple and rapid means for concentrating PI from a phospholipid mixture.
