In the present work, canola oil cake was used as a substrate for lipase production employing Ganoderma lucidum. The enzyme was isolated and partially purified using factional precipitation, ion exchange chromatography and gel filtration. The purified lipase had a specific activity of 33262 U/mg proteins with 2.26 % recovery. The pH and temperature optima of the lipase were 8.5 and 35 °C indicating its alkaline nature. The Michaelis-Menten parameters Km and Vmax were found to be 0.74 mM and 4762 µmol/min respectively. Energy of activation (Ea) for PNPP hydrolysis was found to be 12.80 kJ/mol. Thermostability studies of the enzyme at various temperatures showed that the enzyme denaturation followed pseudo-first-order kinetic. Effects of various metal ions, surfactants and organic solvents were investigated. The purified lipase had the highest hydrolytic activity for waste oil indicating its potential for wide application in oleochemical and biotechnological industries.