Cantarella L, Alfani F, Cantarella M
Department of Industrial Engineering, University of Cassino, Italy.
Enzyme Microb Technol. 1993 Oct;15(10):861-7. doi: 10.1016/0141-0229(93)90098-m.
Enzyme storage stability and hydrolysis yield were measured in experiments carried out with three model hydrolytic enzymes: acid phosphatase (EC 3.1.3.2), beta-glucosidase (EC 3.2.1.4), and beta-fructofuranosidase (EC 3.2.1.26) entrapped in hydrogels of poly(2-hydroxyethyl methacrylate). Runs were performed at 30 degrees C, under intensive stirring (500 rev min-1), in 50% v/v biphasic media prepared with buffer and organic solvents, whose log P value varied from 0.68 to 8.8. Storage stability was also monitored in the pure solvents. The small average particle size (125-210 microns) and the intensive stirring eliminate hindrances of intra- and interphase mass transfer resistances. The hydrophilic matrix protects the enzymes against thermal and chemical deactivation, thus allowing good production per unit weight of biocatalyst. In biphasic media, storage stability, with the exception of acid phosphatase, was not dependent on solvent polarity. On the contrary, a significant trend was observed when the enzymes were stored in neat organic solvents.
在用三种模型水解酶进行的实验中测定了酶的储存稳定性和水解产率，这三种酶分别是：酸性磷酸酶（EC 3.1.3.2）、β-葡萄糖苷酶（EC 3.2.1.4）和β-呋喃果糖苷酶（EC 3.2.1.26），它们被包埋在聚（甲基丙烯酸2-羟乙酯）水凝胶中。实验在30℃下进行，剧烈搅拌（500转/分钟），在由缓冲液和有机溶剂配制的50% v/v双相介质中进行，其log P值在0.68至8.8之间变化。还在纯溶剂中监测了储存稳定性。平均粒径小（125 - 210微米）和剧烈搅拌消除了相间和相内传质阻力的阻碍。亲水性基质保护酶免受热失活和化学失活，从而使每单位重量的生物催化剂具有良好的产量。在双相介质中，除酸性磷酸酶外，储存稳定性不依赖于溶剂极性。相反，当酶储存在纯有机溶剂中时，观察到显著的趋势。
