Purification and properties of lipase from Penicillium simplicissimum.
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.
Sztajer
H
H
Gesellschaft für Biotechnologische Forschung, Braunschweig, Germany.
Lünsdorf
H
H
Erdmann
H
H
Menge
U
U
Schmid
R
R
D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction; D006031:Glycosylation; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000037:antagonists & inhibitors / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D008854:Microscopy, Electron; D010407:Penicillium / Q000378:metabolism*; D013696:Temperature; D014304:Triolein / Q000494:pharmacology
D000596:Amino Acids; D014304:Triolein; D008049:Lipase