Nature Communications · 2015 · 681 citations · 31 references
Life SciencesBiotechnologyChemical EngineeringBiocatalysisCatalysisEnzymologyBiocatalyst EngineeringEnzymatic CatalysisEnzyme ImmobilizationEnzyme StabilityImmobilized EnzymesNanocatalysisCatalytic EfficiencyCatalytic StabilityEncapsulationEnzyme Aggregation PreventionEnzyme EncapsulationEnzymesMetal-organic FrameworksOperational Stability
Enzymatic catalytic processes possess great potential in chemical manufacturing, including pharmaceuticals, fuel production and food processing. However, the engineering of enzymes is severely hampered due to their low operational stability and difficulty of reuse. Here, we develop a series of stable metal-organic frameworks with rationally designed ultra-large mesoporous cages as single-molecule traps (SMTs) for enzyme encapsulation. With a high concentration of mesoporous cages as SMTs, PCN-333(Al) encapsulates three enzymes with record-high loadings and recyclability. Immobilized enzymes that most likely undergo single-enzyme encapsulation (SEE) show smaller Km than free enzymes while maintaining comparable catalytic efficiency. Under harsh conditions, the enzyme in SEE exhibits better performance than free enzyme, showing the effectiveness of SEE in preventing enzyme aggregation or denaturation. With extraordinarily large pore size and excellent chemical stability, PCN-333 may be of interest not only for enzyme encapsulation, but also for entrapment of other nanoscaled functional moieties. Enzymatic catalytic processes have great industrial potential, although their application is hampered by stability and reuse issues. Here, the authors report metal-organic frameworks with rationally designed single-molecule traps for enzyme encapsulation, and evaluate the activity of the confined enzymes.
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