Purification and substrate specificities of phospholipase A and B of Sclerotinia fungus.

The phospholipase of Sclerotinia fungus was separated by the paperelectrophoresis method into three fractions, of which one component is phospholipase A and the others phospholipase B. These enzymes could be isolated also by the column chromatography using anion exchange resin Duolite A 2 and DEAE cellulose. The former and one of the latter enzymes were obtained in a crystalline form from its solution saturated with ammonium sulfate. The investigation of substrate specificities of these enzymes has shown that the two phospholipase B hydrolyze a commercial soybean lecithin, and one of them can also attack egg-yolk lecithin without addition of any activating lipides.