Rees G D, da Graca Nascimento M, Jenta T R, Robinson B H
School of Chemical Sciences, University of East Anglia, Norwich, U.K.
Biochim Biophys Acta. 1991 Apr 9;1073(3):493-501. doi: 10.1016/0304-4165(91)90221-2.
Lipase from three different sources has been immobilised in microemulsion-based gels (MBGs) with retention of catalytic activity. Such lipase-containing MBGs prove to be novel solid-phase catalysts for use in apolar organic solvents such as n-heptane. Using these systems, preparative-scale synthesis of a wide variety of esters under mild conditions was possible with products easily isolated and obtained in high yield. Stereoselective esterification of octan-2-ol was observed for all three lipases with Chromobacterium viscosum (CV) lipase yielding product with an enantiomeric excess of 92%. Repeated usage of a CV lipase-containing MBG resulted in a visually unchanged gel whose activity was 75% of the initial value after 30 days. The sectioned MBGs were well suited for use in column flow reactors and were also found to be effective esterification catalysts at temperatures as low as -20 degrees C.
来自三种不同来源的脂肪酶已被固定在基于微乳液的凝胶（MBG）中，并保留了催化活性。这种含脂肪酶的MBG被证明是用于非极性有机溶剂（如正庚烷）的新型固相催化剂。使用这些体系，可以在温和条件下进行多种酯的制备规模合成，产物易于分离且产率高。对所有三种脂肪酶都观察到了2-辛醇的立体选择性酯化反应，其中粘质色杆菌（CV）脂肪酶产生的对映体过量产物为92%。含CV脂肪酶的MBG重复使用后，凝胶外观无明显变化，30天后其活性为初始值的75%。切片的MBG非常适合用于柱流式反应器，并且发现在低至-20℃的温度下也是有效的酯化催化剂。
