Abstract
The immobilization of enzymes in metal–organic frameworks (MOFs) with preserved biofunctionality paves a promising way to solve problems regarding the stability and reusability of enzymes. However, the rational design of MOF-based biocomposites remains a considerable challenge as very little is known about the state of the enzyme, the MOF support, and their host–guest interactions upon immobilization. In this study, we elucidate the detailed host–guest interaction for MOF immobilized enzymes in the biointerface. Two enzymes with different sizes, lipase and insulin, have been immobilized in a mesoporous PCN-333(Al) MOF. The dynamic changes of local structures of the MOF host and enzyme guests have been experimentally revealed for the existence of the confinement effect to enzymes and van der Waals interaction in the biointerface between the aluminum oxo-cluster of the PCN-333 and the -NH2 species of enzymes. This kind of host–guest interaction renders the immobilization of enzymes in PCN-333 with high affinity and highly preserved enzymatic bioactivity.
[Graphic presents]
[Graphic presents]
Original language | English |
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Pages (from-to) | 2172-2181 |
Number of pages | 10 |
Journal | JACS Au |
Volume | 1 |
Issue number | 12 |
Early online date | 15 Nov 2021 |
DOIs | |
Publication status | Published - 27 Dec 2021 |
Bibliographical note
Copyright the Author(s) 2021. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.Keywords
- metal-organic frameworks
- enzyme immobilization
- solid-state NMR
- biointerface interaction
- biocatalysis