Production of specialty chemicals increasingly makes use of the enzyme catalysts in organic solvents, and Novozym 435 (N435) is among most often applied. However, its polymeric skeleton is unstable in many solvents. In this context we report the results of a more systematic study of the biocatalysts, fabricated using highly porous siliceous pellets/enzyme carriers (MH, 4 cm³ g⁻¹ total pore volume, 310 m² g⁻¹ surface area), grafted with octyl (-O), amino (-A) and octyl and amino (-OA) groups, to attach the enzyme - CALB lipase. The catalysts were deployed in a rotating bed reactor (RBR) and tested in hydrolysis of p-nitrophenyl acetate, and esterification of levulinic acid. Performance of the system was compared with the same RBR filled with N435. N435 appeared the most active in both reactions, when activity was related to bulk mass of the catalysts, mainly owing to very large enzyme load. But its pore structure degraded in many typical solvents already after 24 h of soaking, whereas no significant change in MH-O and MH-OA activity was detected. Irrespective of the solvent and reaction, the highest specific activity of the enzyme featured MH-O. However, a significant enzyme leaching from MH-O observed in a hydrolytic reaction, in stark contrast to MH-OA which came second in specific activity, point to MH-OA as the catalyst of choice for hydrolytic reactions. In esterification reaction the MH-O lipase was not only most active but it was also quite stable. Therefore, MH-O appears the most suitable production system for the reactions carried out in organic solvents.

特种化学品的生产越来越多地在有机溶剂中使用酶催化剂，Novozym 435（N435）是最常使用的。但是，其聚合物骨架在许多溶剂中不稳定。在这方面，我们报告的生物催化剂进行更系统的研究的结果，使用高多孔硅质粒料/酶的载体制造（MH，4厘米³ 克^-1的总孔体积，310米² 克^-1表面积），接枝有辛基（-O），氨基（-A）以及辛基和氨基（-OA）基团，以连接酶-CALB脂肪酶。将催化剂部署在旋转床反应器（RBR）中，并测试乙酸对硝基苯酯的水解和乙酰丙酸的酯化。将系统性能与填充N435的同一RBR进行了比较。N435在两个反应中都表现出最强的活性，这是因为活性与催化剂的总质量有关，这主要是由于酶的负载量很大。但是在浸泡24小时后，它的孔结构已经在许多典型溶剂中降解，而未检测到MH-O和MH-OA活性发生显着变化。不论溶剂和反应如何，该酶的最高比活性均以MH-O为特征。但是，在水解反应中观察到从MH-O大量浸出的酶，与比活第二位的MH-OA形成鲜明对比的是，MH-OA是水解反应的首选催化剂。在酯化反应中，MH-O脂肪酶不仅活性最高，而且非常稳定。因此，MH-O似乎是最适合在有机溶剂中进行反应的生产系统。