Cargando…
Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives
Oxidoreductases are a wide class of enzymes that can catalyze biological oxidation and reduction reactions. Nowadays, oxidoreductases play a vital part in most bioenergetic metabolic pathways, which have important applications in biodegradation, bioremediation, environmental applications, as well as...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10574266/ https://www.ncbi.nlm.nih.gov/pubmed/37834709 http://dx.doi.org/10.3390/ma16196572 |
_version_ | 1785120653654884352 |
---|---|
author | Yang, Pengyan Yang, Wenhui Zhang, Haiyang Zhao, Rui |
author_facet | Yang, Pengyan Yang, Wenhui Zhang, Haiyang Zhao, Rui |
author_sort | Yang, Pengyan |
collection | PubMed |
description | Oxidoreductases are a wide class of enzymes that can catalyze biological oxidation and reduction reactions. Nowadays, oxidoreductases play a vital part in most bioenergetic metabolic pathways, which have important applications in biodegradation, bioremediation, environmental applications, as well as biosensors. However, free oxidoreductases are not stable and hard to be recycled. In addition, cofactors are needed in most oxidoreductases catalyze reactions, which are so expensive and unstable that it hinders their industrial applications. Enzyme immobilization is a feasible strategy that can overcome these problems. Recently, metal–organic frameworks (MOFs) have shown great potential as support materials for immobilizing enzymes due to their unique properties, such as high surface-area-to-volume ratio, chemical stability, functional designability, and tunable pore size. This review discussed the application of MOFs and their composites as immobilized carriers of oxidoreductase, as well as the application of MOFs as catalysts and immobilized carriers in redox reactions in the perspective of the function of MOFs materials. The paper also focuses on the potential of MOF carrier-based oxidoreductase immobilization for designing an enzyme cascade reaction system. |
format | Online Article Text |
id | pubmed-10574266 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-105742662023-10-14 Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives Yang, Pengyan Yang, Wenhui Zhang, Haiyang Zhao, Rui Materials (Basel) Review Oxidoreductases are a wide class of enzymes that can catalyze biological oxidation and reduction reactions. Nowadays, oxidoreductases play a vital part in most bioenergetic metabolic pathways, which have important applications in biodegradation, bioremediation, environmental applications, as well as biosensors. However, free oxidoreductases are not stable and hard to be recycled. In addition, cofactors are needed in most oxidoreductases catalyze reactions, which are so expensive and unstable that it hinders their industrial applications. Enzyme immobilization is a feasible strategy that can overcome these problems. Recently, metal–organic frameworks (MOFs) have shown great potential as support materials for immobilizing enzymes due to their unique properties, such as high surface-area-to-volume ratio, chemical stability, functional designability, and tunable pore size. This review discussed the application of MOFs and their composites as immobilized carriers of oxidoreductase, as well as the application of MOFs as catalysts and immobilized carriers in redox reactions in the perspective of the function of MOFs materials. The paper also focuses on the potential of MOF carrier-based oxidoreductase immobilization for designing an enzyme cascade reaction system. MDPI 2023-10-06 /pmc/articles/PMC10574266/ /pubmed/37834709 http://dx.doi.org/10.3390/ma16196572 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Yang, Pengyan Yang, Wenhui Zhang, Haiyang Zhao, Rui Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives |
title | Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives |
title_full | Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives |
title_fullStr | Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives |
title_full_unstemmed | Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives |
title_short | Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives |
title_sort | metal–organic framework for the immobilization of oxidoreductase enzymes: scopes and perspectives |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10574266/ https://www.ncbi.nlm.nih.gov/pubmed/37834709 http://dx.doi.org/10.3390/ma16196572 |
work_keys_str_mv | AT yangpengyan metalorganicframeworkfortheimmobilizationofoxidoreductaseenzymesscopesandperspectives AT yangwenhui metalorganicframeworkfortheimmobilizationofoxidoreductaseenzymesscopesandperspectives AT zhanghaiyang metalorganicframeworkfortheimmobilizationofoxidoreductaseenzymesscopesandperspectives AT zhaorui metalorganicframeworkfortheimmobilizationofoxidoreductaseenzymesscopesandperspectives |