Sztajer H, Borkowski J, Sobiech K
Institute of Organic and Physical Chemistry, Technical University of Wroclaw, Poland.
Biotechnol Appl Biochem. 1991 Feb;13(1):65-71.
Lipase (triacylglycerol lipase, EC 3.1.1.3) has been purified from Pseudomonas fluorescens wild strain by chromatography on DEAE-cellulose and octyl-Sepharose CL-4B. The yield was 21% and the specific activity of the purified enzyme 4780 U/mg protein. It showed a Mr of about 45 x 10(4) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme is active over a wide pH range and at 50-55 degrees C.
脂肪酶（三酰基甘油脂肪酶，EC 3.1.1.3）已通过在DEAE-纤维素和辛基-琼脂糖CL-4B上进行色谱法从荧光假单胞菌野生菌株中纯化出来。产率为21%，纯化酶的比活性为4780 U/mg蛋白质。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示其分子量约为45×10⁴。该酶在较宽的pH范围内以及50 - 55摄氏度下具有活性。
