Document Type
Article
Publication Date
2020
Digital Object Identifier (DOI)
https://doi.org/10.1021/acscentsci.0c00687
Abstract
Enzyme immobilization in metal–organic frameworks (MOFs) as a promising strategy is attracting the interest of scientists from different disciplines with the expansion of MOFs’ development. Different from other traditional host materials, their unique strengths of high surface areas, large yet adjustable pore sizes, functionalizable pore walls, and diverse architectures make MOFs an ideal platform to investigate hosted enzymes, which is critical to the industrial and commercial process. In addition to the protective function of MOFs, the extensive roles of MOFs in the enzyme immobilization are being well-explored by making full use of their remarkable properties like well-defined structure, high porosity, and tunable functionality. Such development shifts the focus from the exploration of immobilization strategies toward functionalization. Meanwhile, this would undoubtedly contribute to a better understanding of enzymes in regards to the structural transformation after being hosted in a confinement environment, particularly to the orientation and conformation change as well as the interplay between enzyme and matrix MOFs. In this Outlook, we target a comprehensive review of the role diversities of the host matrix MOF based on the current enzyme immobilization research, along with proposing an outlook toward the future development of this field, including the representatives of potential techniques and methodologies being capable of studying the hosted enzymes.
Rights Information
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
ACS Central Science, v. 6, issue 9, p. 1497-1506
This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
Scholar Commons Citation
Wang, Xiaoliang; Lan, Pui Ching; and Ma, Shengqian, "Metal–Organic Frameworks for Enzyme Immobilization: Beyond Host Matrix Materials" (2020). Chemistry Faculty Publications. 113.
https://digitalcommons.usf.edu/chm_facpub/113