Abstract Phospholipase A activity has been characterized in the conidia of Neurospora crassa. It has been observed that almost the entire phospholipase A activity in the conidia could be leached out by washing these with aqueous solution. The properties of this exocellular phospholipase A have been determined. Two distinct phospholipases have been fractionated from the “conidial water washing” by gel chromatography using Sephadex G-100. Using specific substrate, 1-stearyl-2-oleoyl lecithin, the predominant phospholipase activity in the fraction with higher molecular weight has been found to be due to phospholipase A 1 and that in fraction with lower molecular weight has been found to be due to phospholipase A 2. Properties of these two different enzyme fractions have been studied. The most active fraction in the latter gives a single band in 7.5% polyacrylamide gel. Lysophospholipase activity and detergent-stimulated phospholipase D activity have been detected also in the conidia. The effects of different physical and chemical agents on phospholipase A activity in the “conidial water washing” as well as in the purified fractions have been studied.