Abstract
Enzymes capable of performing selective chemical transformations under benign and environmentally friendly conditions are attractive alternatives to synthetic catalysts. The inherent instability of many enzymes is, however, an impediment to their widespread application. Here, we demonstrate that biomimetic crystallization provides a route to metal-organic framework (MOF)-enzyme composites that are stable in aqueous and organic solvents, and can be reused over multiple reaction cycles. We show that for silicatein, an enzyme with established stability challenges, this approach extends the enzymatic half-life at room temperature from one week to one month. We also demonstrate how changes in the MOF structure affect the solution processability, driving enhanced catalytic performance. Biomimetic MOF crystallization thus represents a robust approach to the stabilization of biocatalysts for process intensification.