Insights into the Interaction between Immobilized Biocatalysts and Metal–Organic Frameworks: A Case Study of PCN-333
Files
(Published version)
Date
2021
Authors
Yang, W.
Liang, W.
O’Dell, L.A.
Toop, H.D.
Maddigan, N.
Zhang, X.
Kochubei, A.
Doonan, C.J.
Jiang, Y.
Huang, J.
Editors
Advisors
Journal Title
Journal ISSN
Volume Title
Type:
Journal article
Citation
JACS Au, 2021; 1(12):2172-2181
Statement of Responsibility
Wenjie Yang, Weibin Liang, Luke A. O, Dell, Hamish D. Toop, Natasha Maddigan, Xingmo Zhang, Alena Kochubei, Christian J. Doonan, Yijiao Jiang, and Jun Huang
Conference Name
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 PCN333(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.
School/Discipline
Dissertation Note
Provenance
Description
Access Status
Rights
© 2021 The Authors. Published by American Chemical Society. Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)