Centre for Chemistry and Biotechnology, School of Life and Environmental Sciences, Deakin University, Geelong, Victoria 3216, Australia.
Institute for Frontier Materials, Deakin University, Geelong, Victoria 3216, Australia.
Langmuir. 2023 Jun 6;39(22):7979-7985. doi: 10.1021/acs.langmuir.3c00879. Epub 2023 May 25.
Rationally tailoring a controlled spatial organization of enzymes in a nanoarchitecture for multi-enzyme cascade reactions can enhance the catalytic efficiency via substrate channeling. However, attaining substrate channeling is a grand challenge, requiring sophisticated techniques. Herein, we report facile polymer-directed metal-organic framework (MOF)-based nanoarchitechtonics for realizing a desirable enzyme architecture with significantly enhanced substrate channeling. The new method involves the use of poly(acrylamide-co-diallyldimethylammonium chloride) (PADD) as a modulator in a one-step process for simultaneous MOF synthesis and co-immobilization of enzymes (GOx and HRP). The resultant enzymes-PADD@MOFs constructs showed a closely packed nanoarchitecture with enhanced substrate channeling. A transient time close to 0 s was observed, owing to a short diffusion path for substrates in a 2D spindle-shaped structure and their direct transfer from one enzyme to another. This enzyme cascade reaction system showed a 3.5-fold increase in catalytic activity in comparison to free enzymes. The findings provide a new insight into using polymer-directed MOF-based enzyme nanoarchitectures to improve catalytic efficiency and selectivity.
理性设计纳米结构中酶的可控空间组织以用于多酶级联反应，可以通过底物通道化来提高催化效率。然而，实现底物通道化是一个巨大的挑战，需要复杂的技术。在此，我们报告了一种简便的聚合物导向的金属-有机骨架（MOF）基纳米架构方法，用于实现具有显著增强的底物通道化的理想酶结构。该新方法涉及在一步法中使用聚丙烯酰胺-co-二烯丙基二甲基氯化铵（PADD）作为调节剂，同时进行 MOF 合成和酶（GOx 和 HRP）的共固定。所得酶-PADD@MOFs 结构表现出增强的底物通道化的紧密堆积纳米结构。由于在 2D 纺锤形结构中底物的扩散路径较短，并且它们可以直接从一种酶转移到另一种酶，因此观察到瞬态时间接近 0 s。与游离酶相比，该酶级联反应体系的催化活性提高了 3.5 倍。这些发现为利用聚合物导向的基于 MOF 的酶纳米架构来提高催化效率和选择性提供了新的见解。
