In Situ Immobilization of Multi-Enzymes for Enhanced Substrate Channeling of Enzyme Cascade Reactions: A Nanoarchitectonics Approach by Directed Metal-Organic Frameworks

Rationallytailoring a controlled spatial organization of enzymesin a nanoarchitecture for multi-enzyme cascade reactions can enhancethe catalytic efficiency via substrate channeling. However, attainingsubstrate channeling is a grand challenge, requiring sophisticatedtechniques. Herein, we report facile polymer-directed metal-organicframework (MOF)-based nanoarchitechtonics for realizing a desirableenzyme architecture with significantly enhanced substrate channeling.The new method involves the use of poly(acrylamide-co-diallyldimethylammoniumchloride) (PADD) as a modulator in a one-step process for simultaneousMOF synthesis and co-immobilization of enzymes (GOx and HRP). Theresultant enzymes-PADD@MOFs constructs showed a closely packed nanoarchitecturewith enhanced substrate channeling. A transient time close to 0 swas observed, owing to a short diffusion path for substrates in a2D spindle-shaped structure and their direct transfer from one enzymeto another. This enzyme cascade reaction system showed a 3.5-foldincrease in catalytic activity in comparison to free enzymes. Thefindings provide a new insight into using polymer-directed MOF-basedenzyme nanoarchitectures to improve catalytic efficiency and selectivity.

Automated summary

A facile polymer-directed metal-organic framework (MOF)-based nanoarchitechtonics was developed to enhance the catalytic efficiency of multi-enzyme cascade reactions through substrate channeling. The new method involved the simultaneous synthesis of MOF and co-immobilization of enzymes, resulting in a closely packed nanoarchitecture with enhanced substrate channeling. The enzyme cascade reaction system showed a 3.5-fold increase in catalytic activity compared to free enzymes.