[Characteristics of lipases in the culture fluid of Penicillium roqueforti].
Lipases were isolated from the cultural broth of Penicillium roqueforti 141, purified and their properties were studied. The lipases differed in their amino acid composition and had a high content of polar amino acids , in particular aspartic and glutamic acids. The lipases contained also carbohydrates (1.4-3.3%): mannose, xylose and glucosamine. The lipases were stable to heating (up to 55 degrees C) and within a wide pH range. The optimal activity of lipases I and III was observed at 40 degrees C and pH 7.0, that of lipase II at 45 degrees C and pH 6.0. The effect of metal ions and various inhibitors on the activity of the lipases was studied. Ca2+, Mg2+ and Fe2+ ions did not activate the lipases. These were inhibited by a broad spectrum of reagents for sulfhydryl groups and by a phosphoorganic compound. This fact suggest that the lipases belong to "serine" enzymes containing sulfhydryl groups.
D000596:Amino Acids / Q000032:analysis; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D010407:Penicillium / Q000201:enzymology*; D011489:Protein Denaturation; D013696:Temperature
D000596:Amino Acids; D008049:Lipase
Kharakteristiki lipaz, soderzhashchikhsia v kul'tural'noĭ zhidkosti Penicillium roqueforti.