Purification and properties of lipase from Penicillium simplicissimum

doi:10.1016/0005-2760(92)90137-K

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism

Volume 1124, Issue 3, 25 March 1992, Pages 253-261

Biochimica et Biophy...

https://doi.org/10.1016/0005-2760(92)90137-K Get rights and content

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.

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Regular paperPurification and properties of lipase from Penicillium simplicissimum

Abstract

Lipolytic enzymes

Lipases

Appl. Microbiol. Biotechnol.

Botechnol. Bioeng.

Biotechnol. Bioeng.

Ann. NY Acad. Sci.

Agric. Biol. Chem.

J. Am. Oil Chem. Soc.

J. Am. Oil Chem. Soc.

J. Org. Chem.

J. Am. Oil Chem. Soc.

J. Gen. Microbiol.

Lipids

Ann. NY Acad. Sci.

Lipids

Biotechnol. Lett.

J. Biochem.

Food Sci.

Microbios. Lett.

Regular paper
Purification and properties of lipase from Penicillium simplicissimum