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In studies of characterization of phospholipases pro duced by C. centrifugum IAM 9028, we have purified phospholipase A,,1) phospholipase B2) and lysophos pholipase2) from the culture medium and have investi gated their properties. In this paper, we describe some properties of intracellular phospholipases in C. centri fugum and compare them with extracellular phos pholipases. C. centrifugum IAM 9028 was cultured in medium containing 4% heat-treated brewer's yeast, as described previously.1) After 4 days incubation, mycelia were collected by centrifugation and washed three times with 0.9% NaC1 solution. Then the mycelia were homo genized by a Waring blender in 3 volumes of 0.05M Tris-HCl buffer, pH 7.1. The homogenate was centri fuged at 20,000•~g for 20min. To the supernatant solution was added solid ammonium sulfate equal to 100% saturation, and this mixture was stirred overnight. The resulting precipitate was collected by cen trifugation and dialyzed against 0.05M Tris-HCl buffer,

Occurrence and properties of intracellular phospholipases in Corticium centrifugum.