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- Title
Rapid mechanochemical encapsulation of biocatalysts into robust metal–organic frameworks.
- Authors
Wei, Tz-Han; Wu, Shi-Hong; Huang, Yi-Da; Lo, Wei-Shang; Williams, Benjamin P.; Chen, Sheng-Yu; Yang, Hsun-Chih; Hsu, Yu-Shen; Lin, Zih-Yin; Chen, Xin-Hua; Kuo, Pei-En; Chou, Lien-Yang; Tsung, Chia-Kuang; Shieh, Fa-Kuen
- 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 β-glucosidase, invertase, β-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. Metal–organic frameworks (MOFs) are attractive for encapsulating enzymes for industrial purposes because they can increase selectivity, stability, and/or activity of the enzymes. Here, the authors developed an economical solid-state mechanochemical method to encapsulate enzymes during MOF synthesis.
- Subjects
ENCAPSULATION (Catalysis); ENZYMES; METAL-organic frameworks; GLUCOSIDASES; CATALASE
- Publication
Nature Communications, 2019, Vol 10, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-019-12966-0