Some properties of lipolytic enzymes of a microsomal fraction of two Polish varieties of rapeseed were qualified. Enzymes extracts were prepared front germinated rapeseeds of two varieties: double improved - Bolko and high erucic - Skrzeszowicki. The lipase was purified by ultracentifuge. The obtained supernatant was used to chracterise the lipase and further to purify by a column chromatography method, using the following carriers: Sephadex G-100, Sephacryl S-300, DEAE sephadex A-50 and Q Sepharose. Examined enzymatic extracts showed two optima of lipolytic activity: pH 7.5 and pH 9.0. The highest degree of hydrolysis of tributyrylglicerol (TC 4 : 0) revealed lipases of the Bolko variety seeds at 30°C, and lipases of the Skrzeszowicki seeds at 40°C. At the temperature 30 - 40°C lipases maintained approx. 89 % to 93 % of their maximum activity. However, at 25°C and 50°C their activity was reduced to approx 20 %. When the temperature was above 40°C, thermal inactivation of lipolytic enzymes from two varieties progressed in two stages. Examined lipases maintained 20 % to 30 % of their initial activity, after storing them for 1 h at 60°C. During the purification of lipases, carried out by a column chromatography method, the most favourable results were obtained using molecular filtration on Sephadex G-100 gel.