Key Laboratory of Mesoscopic Chemistry of MOE, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210093, China.
J Colloid Interface Sci. 2012 Jul 1;377(1):497-503. doi: 10.1016/j.jcis.2012.03.057. Epub 2012 Mar 28.
New concept on the promotion of immobilization and catalytic activity of enzyme on mesoporous silica through template micelles is proposed and realized in this paper. Proper P123 templates are controllable retained in the as-synthesized SBA-15, not only to anchor the horseradish peroxidase (HRP) guest, but also to establish the crowding-like microenvironment around the enzyme. The influence of retaining templates on the pore structure of SBA-15, immobilization, and catalytic activity of HRP is studied, and the possible process of template removal is proposed. Ethanol refluxing of 6 h is conformable to prepare the optimal mesoporous support characterized with the retained templates of about 8%. With the assistance of retained templates in SBA-15, up to 49 mg g(-1) of HRP can be immobilized, 100% more than that on calcined SBA-15. Furthermore, the thermal stability, the resistance of pH variation and denaturing agent urea, and the recycle usage of HRP immobilized are obviously elevated, paving a novel and low-cost route to develop enzyme catalysts.
本文提出并实现了一种通过模板胶束来提高酶在介孔硅上的固定化和催化活性的新概念。适当的 P123 模板可以在合成的 SBA-15 中被可控地保留，不仅可以锚定辣根过氧化物酶（HRP）客体，还可以在酶周围建立拥挤类似的微环境。研究了保留模板对 SBA-15 的孔结构、HRP 的固定化和催化活性的影响，并提出了模板去除的可能过程。乙醇回流 6 小时是制备最佳介孔载体的合适条件，该载体的保留模板约为 8%。在 SBA-15 中保留模板的辅助下，HRP 的固定化量高达 49mg g(-1)，比煅烧后的 SBA-15 高出 100%。此外，固定化 HRP 的热稳定性、耐 pH 值变化和变性剂脲的能力以及循环使用性能都得到了明显提高，为开发酶催化剂开辟了一条新颖且低成本的途径。
