Using Defect Control to Break the Stability-Activity Trade-Off in Enzyme Immobilization Via Competitive Coordination

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Abstract

Immobilization of enzymes within metal-organic frameworks is a powerful strategy to enhance the long-term usability of labile enzymes. However, the thus-confined enzymes suffer from the trade-off between enhanced stability and reduced activity because of the contradiction between the high crystallinity and the low accessibility. Here, by taking laccase and zeolitic imidazolate framework-8 (ZIF-8) as prototypes, we disclosed an observation that the stability-activity trade-off could be solved by controlling the defects via competitive coordination. Owing to the presence of competitive coordination between laccase and the ligand precursor of ZIF-8, there existed a three-stage process in the de novo encapsulation: nucleation-crystallization-recrystallization. Our results show that the biocomposites collected before the occurrence of recrystallization possessed both increased activity and enhanced stability. The findings here shed new light on the control of defects through the subtle use of competitive coordination, which is of great significance for the engineering application of biomacromolecules.

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