| Title : Purification and properties of lipase from Penicillium simplicissimum - Sztajer_1992_Biochim.Biophys.Acta_1124_253 |
| Author(s) : Sztajer H , Lunsdorf H , Erdmann H , Menge U , Schmid R |
| Ref : Biochimica & Biophysica Acta , 1124 :253 , 1992 |
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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. |
| PubMedSearch : Sztajer_1992_Biochim.Biophys.Acta_1124_253 |
| PubMedID: 1576166 |
Sztajer H, Lunsdorf H, Erdmann H, Menge U, Schmid R (1992)
Purification and properties of lipase from Penicillium simplicissimum
Biochimica & Biophysica Acta
1124 :253
Sztajer H, Lunsdorf H, Erdmann H, Menge U, Schmid R (1992)
Biochimica & Biophysica Acta
1124 :253