Lobyreva L B, Marchenkova A I
Mikrobiologiia. 1981 Jan-Feb;50(1):90-5.
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.
从罗克福特青霉141的培养液中分离出脂肪酶，进行纯化并研究其性质。这些脂肪酶的氨基酸组成不同，极性氨基酸含量较高，尤其是天冬氨酸和谷氨酸。脂肪酶还含有碳水化合物（1.4 - 3.3%）：甘露糖、木糖和氨基葡萄糖。脂肪酶在加热（高达55摄氏度）和较宽的pH范围内稳定。脂肪酶I和III的最佳活性在40摄氏度和pH 7.0时观察到，脂肪酶II的最佳活性在45摄氏度和pH 6.0时观察到。研究了金属离子和各种抑制剂对脂肪酶活性的影响。Ca2 +、Mg2 +和Fe2 +离子不激活脂肪酶。它们被多种巯基试剂和一种有机磷化合物抑制。这一事实表明这些脂肪酶属于含巯基的“丝氨酸”酶。
