Inada Y, Nishimura H, Takahashi K, Yoshimoto T, Saha A R, Saito Y
Biochem Biophys Res Commun. 1984 Jul 31;122(2):845-50. doi: 10.1016/s0006-291x(84)80111-4.
Lipoprotein lipase, which catalyzes hydrolysis of emulsified triglycerides or water-insoluble esters, was modified with 2,4-bis(o-methoxy-polyethylene glycol)-6-chloro-s-triazine(activated PEG2). The modified lipase, in which 55% of the total amino groups in the lipase molecule, was soluble in organic solvents such as benzene, toluene, chloroform and dioxane. The modified lipase could catalyze ester synthesis reaction in benzene. When very hydrophobic substrates of lauryl alcohol and stearic acid were used, the ester synthesis reaction proceeded efficiently in the transparent benzene solution with the maximum activity of approximate 5.0 mumoles/min/mg of protein. Ester exchange and aminolysis reactions were also conducted with the modified lipase in benzene.
脂蛋白脂肪酶可催化乳化甘油三酯或水不溶性酯的水解，它用2,4-双（邻甲氧基聚乙二醇）-6-氯-s-三嗪（活化聚乙二醇2）进行了修饰。修饰后的脂肪酶分子中55%的总氨基可溶于苯、甲苯、氯仿和二氧六环等有机溶剂。修饰后的脂肪酶可在苯中催化酯合成反应。当使用月桂醇和硬脂酸等疏水性很强的底物时，酯合成反应在透明的苯溶液中高效进行，最大活性约为5.0微摩尔/分钟/毫克蛋白质。酯交换反应和氨解反应也在苯中用修饰后的脂肪酶进行。
