Mase T, Matsumiya Y, Akiba T
Research and Development Division, Amano Pharmaceutical Co., Ltd., Aichi, Japan.
Biosci Biotechnol Biochem. 1995 Sep;59(9):1771-2. doi: 10.1271/bbb.59.1771.
The extracellular lipase from Fusarium sp. YM-30 was purified by a procedure involving ultrafiltration, ammonium sulfate precipitation, and DEAE-Toyopearl 650M, CM-Toyopearl 650M, and Butyl-Toyopearl 650M column chromatographies. The purified lipase was homogeneous with 12kDa of molecular mass by SDS-PAGE, and had high specificities for mono- and diacylglycerols, but low toward triacylglycerols. The enzyme had maximum activity at pH 7.0 to 8.0 and 37 degrees C, and hydrolyzed digalactosyl diglyceride too.
通过包括超滤、硫酸铵沉淀以及DEAE - 托普雷斯650M、CM - 托普雷斯650M和丁基 - 托普雷斯650M柱色谱的步骤，对镰孢菌属YM - 30的胞外脂肪酶进行了纯化。经SDS - PAGE分析，纯化后的脂肪酶分子量为12kDa，呈均一性，对单酰甘油和二酰甘油具有高特异性，但对三酰甘油的特异性较低。该酶在pH 7.0至8.0以及37℃时具有最大活性，并且也能水解二半乳糖基二甘油酯。
