The objective of this work was to determine some properties of lipase synthesised by Rhizopus cohnii. Using hydrophobic chromatography, the lipase was found to have a hydrophobic nature. On a basis of gel filtration through Sephacryl S-300 HR and ultrafiltration, the molecular weight of lipase was determined to be about 30 000 Da. The lipase was observed to show the strongest affinity towards the substrates with long carbon chain (K_m = 0.2 mM) and the weakest one towards short-carbon chain substrates (K_m = 3. 0 mM). The ionic detergent sodium deoxycholate in the concentration of 0.1% did not decrease the lipase activity, that was, however, strongly inhibited by another ionic detergent dodecyl sulfate and non-ionic detergents Triton X-100 and Tween 80 at the concentration as small as 0.05%. The losses of lipase activity for the preparations stored for ten months ranged from 11.5 to 17.0%, depending on the preparation. The characterised lipase preparation was, basically, homogenous since the lipolytic activity predominated and other examined enzymes were present in trace amounts.