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. 1992 Mar 25;1124(3):253-61.
doi: 10.1016/0005-2760(92)90137-k.

Purification and properties of lipase from Penicillium simplicissimum

H Sztajer  1 , H Lünsdorf, H Erdmann, U Menge, R Schmid
Affiliations

Purification and properties of lipase from Penicillium simplicissimum

H Sztajer et al. Biochim Biophys Acta. .

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 56,000 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 degrees C for 15 min. The optimum assay conditions were 37 degrees 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.

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