Hierarchically Engineered Mesoporous Metal-Organic Frameworks toward Cell-free Immobilized Enzyme Systems


Li, Peng, Chen, Qishui, Wang, Timothy C, Vermeulen, Nicolaas A, Mehdi, B Layla ORCID: 0000-0002-8281-9524, Dohnalkoya, Alice, Browning, Nigel D ORCID: 0000-0003-0491-251X, Shen, Dengke, Anderson, Ryther, Gomez-Gualdron, Diego A et al (show 5 more authors) (2018) Hierarchically Engineered Mesoporous Metal-Organic Frameworks toward Cell-free Immobilized Enzyme Systems. Chem, 4 (5). pp. 1022-1034.

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Abstract

Highly efficient cell-free enzymatic systems are typically difficult to achieve in traditional immobilized enzyme systems because of the lack of optimal spatial control of enzyme localization, substrate and product diffusion, and enzyme and coenzyme accessibility. Here, we report a strategy for expanding the pore apertures (from 3.3 to 6.7 nm) of a series of Zr-based metallic-organic frameworks (MOFs) (termed NU-100x, x = 3, 4, 5, 6, 7) with interconnected hierarchical pores by maintaining precise control of torsional angles associated with the linkers. As a proof of concept, we use the expanded NU-100x MOF structures to encapsulate lactate dehydrogenase (LDH) and demonstrate the use of the captured protein in a cell-free biosynthetic catalytic system. Remarkably, LDH immobilized in the large pores of the MOF is accessible to nicotinamide adenine dinucleotide coenzymes (NAD and NADH), allowing for in situ coenzyme regeneration leading to higher activity than that of the free enzyme.

Item Type: Article
Uncontrolled Keywords: metal-organic framework, enzyme immobilization, cell-free enzyme systems, coenzyme regeneration, isoreticular chemistry, csq-net, hierarchical mesopores, coenzyme accessibility
Depositing User: Symplectic Admin
Date Deposited: 23 Nov 2018 15:08
Last Modified: 19 Jan 2023 01:12
DOI: 10.1016/j.chempr.2018.03.001
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3028833
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