Lei Chenghong, Shin Yongsoon, Liu Jun, Ackerman Eric J
Pacific Northwest National Laboratory, Richland, Washington 99352, USA.
J Am Chem Soc. 2002 Sep 25;124(38):11242-3. doi: 10.1021/ja026855o.
The enzyme organophosphorus hydrolase (OPH) was spontaneously entrapped in carboxylethyl- or aminopropyl-functionalized mesoporous silica with rigid, uniform open-pore geometry (30 nm). This approach yielded larger amounts of protein loading and much higher specific activity of the enzyme when compared to the unfunctionalized mesoporous silica and normal porous silica with the same pore size. When OPH was incubated with the functionalized mesoporous silica, protein molecules were sequestered in or excluded from the porous material, depending on electrostatic interaction with the charged functional groups. OPH entrapped in the organically functionalized nanopores showed an exceptional high immobilization efficiency of more than 200% and enhanced stability far exceeding that of the free enzyme in solution. The combination of high protein loading, high immobilization efficiency and stability is attributed to the large and uniform pore structure, and to the optimum environment introduced by the functional groups.
有机磷水解酶（OPH）被自发包埋在具有刚性、均匀开孔几何结构（30纳米）的羧乙基或氨丙基功能化介孔二氧化硅中。与未功能化的介孔二氧化硅以及相同孔径的普通多孔二氧化硅相比，这种方法产生了更大的蛋白质负载量以及更高的酶比活性。当OPH与功能化介孔二氧化硅一起孵育时，蛋白质分子会根据与带电功能基团的静电相互作用被隔离在多孔材料中或被排除在外。包埋在有机功能化纳米孔中的OPH表现出超过200%的极高固定化效率，并且稳定性增强，远远超过溶液中游离酶的稳定性。高蛋白质负载量、高固定化效率和稳定性的结合归因于大而均匀的孔结构以及功能基团引入的最佳环境。
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