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Nat Commun ; 10(1): 5002, 2019 11 01.
Article in English | MEDLINE | ID: mdl-31676820

ABSTRACT

Metal-organic frameworks (MOFs) have recently garnered consideration as an attractive solid substrate because the highly tunable MOF framework can not only serve as an inert host but also enhance the selectivity, stability, and/or activity of the enzymes. Herein, we demonstrate the advantages of using a mechanochemical strategy to encapsulate enzymes into robust MOFs. A range of enzymes, namely ß-glucosidase, invertase, ß-galactosidase, and catalase, are encapsulated in ZIF-8, UiO-66-NH2, or Zn-MOF-74 via a ball milling process. The solid-state mechanochemical strategy is rapid and minimizes the use of organic solvents and strong acids during synthesis, allowing the encapsulation of enzymes into three prototypical robust MOFs while maintaining enzymatic biological activity. The activity of encapsulated enzyme is demonstrated and shows increased resistance to proteases, even under acidic conditions. This work represents a step toward the creation of a suite of biomolecule-in-MOF composites for application in a variety of industrial processes.


Subject(s)
Enzymes, Immobilized/chemistry , Enzymes, Immobilized/metabolism , Metal-Organic Frameworks/chemistry , Metals/chemistry , Biocatalysis , Catalase/chemistry , Catalase/metabolism , Catalase/ultrastructure , Electrophoresis, Polyacrylamide Gel , Enzyme Stability , Enzymes, Immobilized/ultrastructure , Metal-Organic Frameworks/chemical synthesis , Microscopy, Electron, Scanning , Powder Diffraction , beta-Fructofuranosidase/chemistry , beta-Fructofuranosidase/metabolism , beta-Fructofuranosidase/ultrastructure , beta-Galactosidase/chemistry , beta-Galactosidase/metabolism , beta-Galactosidase/ultrastructure , beta-Glucosidase/chemistry , beta-Glucosidase/metabolism , beta-Glucosidase/ultrastructure
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