Technische Universität Berlin, Stranski-Laboratory for Physical and Theoretical Chemistry, Institute of Chemistry, 10623 Berlin, Germany.
Phys Chem Chem Phys. 2012 Jul 21;14(27):9594-600. doi: 10.1039/c2cp40624a. Epub 2012 Jun 8.
The aim of the present work is the use of a water soluble enzyme in an organic solvent, still with a pronounced catalytic activity. Therefore, lipase B from Candida antarctica (CalB) is immobilized within micron-sized thermosensitive p-NIPAM hydrogel particles using a solvent exchange from polar to organic solvents. The absorbed amount of CalB is investigated at different immobilization temperatures. Confocal laser scanning microscopy (CLSM) shows that CalB is homogeneously distributed within the polymer network. An enhanced specific activity of CalB in n-hexane is achieved after immobilization within the p-NIPAM microgels. In order to get information on the supply of the substrate depending on the temperature, the activity is determined at different reaction temperatures. Additionally, the system is stable in the organic solvent, namely n-hexane, and shows a good reusability.
本工作的目的是在有机溶剂中使用一种仍具有显著催化活性的水溶性酶。因此,通过从极性溶剂到有机溶剂的溶剂交换,将南极假丝酵母脂肪酶 B(CalB)固定在微米级热敏 p-NIPAM 水凝胶颗粒内。研究了不同固定化温度下 CalB 的吸附量。共焦激光扫描显微镜(CLSM)表明 CalB 在聚合物网络内均匀分布。CalB 在 p-NIPAM 微凝胶内固定化后,在正己烷中的比活性得到提高。为了获得关于取决于温度的底物供应的信息,在不同的反应温度下确定了活性。此外,该体系在有机溶剂正己烷中稳定,且具有良好的可重复使用性。