Purification and properties of lipase from Penicillium simplicissimum

Abstract A Penicillium simplicissimum strain has been found to produce an inducible extracellular lipase. Triolein was the best inducer for the enzyme production with the highest activity being achieved after 48 h of incubation. The purified lipase showed a molecular weight of 56000 by SDS-PAGE. The enzyme exhibited a high ratio of apolar amino acids. The lipase was stable in the pH range of 5–7 and at 50°C for 15 min. The optimum assay conditions were 37°C and pH 5.0. The enzyme showed a high stability in water immiscible organic solvents. Lipase from P . simplicissimum is nonspecific and hydrolyses each of the three bonds of triacylglycerols.