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Translocation of enzymes into a mesoporous MOF for enhanced catalytic activity under extreme conditions
Enzymatic catalysis is of great importance to the chemical industry. However, we are still scratching the surface of the potential of biocatalysis due to the limited operating range of enzymes in harsh environments or their low recyclability. The role of Metal–Organic Frameworks (MOFs) as active sup...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6469195/ https://www.ncbi.nlm.nih.gov/pubmed/31049190 http://dx.doi.org/10.1039/c9sc00082h |
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author | Navarro-Sánchez, José Almora-Barrios, Neyvis Lerma-Berlanga, Belén Ruiz-Pernía, J. Javier Lorenz-Fonfria, Victor A. Tuñón, Iñaki Martí-Gastaldo, Carlos |
author_facet | Navarro-Sánchez, José Almora-Barrios, Neyvis Lerma-Berlanga, Belén Ruiz-Pernía, J. Javier Lorenz-Fonfria, Victor A. Tuñón, Iñaki Martí-Gastaldo, Carlos |
author_sort | Navarro-Sánchez, José |
collection | PubMed |
description | Enzymatic catalysis is of great importance to the chemical industry. However, we are still scratching the surface of the potential of biocatalysis due to the limited operating range of enzymes in harsh environments or their low recyclability. The role of Metal–Organic Frameworks (MOFs) as active supports to help overcome these limitations, mainly by immobilization and stabilization of enzymes, is rapidly expanding. Here we make use of mild heating and a non-polar medium during incubation to induce the translocation of a small enzyme like protease in the mesoporous MOF MIL-101(Al)-NH(2). Our proteolytic tests demonstrate that protease@MIL-101(Al)-NH(2) displays higher activity than the free enzyme under all the conditions explored and, more importantly, its usability can be extended to extreme conditions of pH and high temperatures. MOF immobilization is also effective in providing the biocomposite with long-term stability, recyclability and excellent compatibility with competing enzymes. This simple, one-step infiltration strategy might accelerate the discovery of new MOF-enzyme biocatalysts that meet the requirements for biotechnological applications. |
format | Online Article Text |
id | pubmed-6469195 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-64691952019-05-02 Translocation of enzymes into a mesoporous MOF for enhanced catalytic activity under extreme conditions Navarro-Sánchez, José Almora-Barrios, Neyvis Lerma-Berlanga, Belén Ruiz-Pernía, J. Javier Lorenz-Fonfria, Victor A. Tuñón, Iñaki Martí-Gastaldo, Carlos Chem Sci Chemistry Enzymatic catalysis is of great importance to the chemical industry. However, we are still scratching the surface of the potential of biocatalysis due to the limited operating range of enzymes in harsh environments or their low recyclability. The role of Metal–Organic Frameworks (MOFs) as active supports to help overcome these limitations, mainly by immobilization and stabilization of enzymes, is rapidly expanding. Here we make use of mild heating and a non-polar medium during incubation to induce the translocation of a small enzyme like protease in the mesoporous MOF MIL-101(Al)-NH(2). Our proteolytic tests demonstrate that protease@MIL-101(Al)-NH(2) displays higher activity than the free enzyme under all the conditions explored and, more importantly, its usability can be extended to extreme conditions of pH and high temperatures. MOF immobilization is also effective in providing the biocomposite with long-term stability, recyclability and excellent compatibility with competing enzymes. This simple, one-step infiltration strategy might accelerate the discovery of new MOF-enzyme biocatalysts that meet the requirements for biotechnological applications. Royal Society of Chemistry 2019-02-28 /pmc/articles/PMC6469195/ /pubmed/31049190 http://dx.doi.org/10.1039/c9sc00082h Text en This journal is © The Royal Society of Chemistry 2019 https://creativecommons.org/licenses/by-nc/3.0/This article is freely available. This article is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported Licence (CC BY-NC 3.0) |
spellingShingle | Chemistry Navarro-Sánchez, José Almora-Barrios, Neyvis Lerma-Berlanga, Belén Ruiz-Pernía, J. Javier Lorenz-Fonfria, Victor A. Tuñón, Iñaki Martí-Gastaldo, Carlos Translocation of enzymes into a mesoporous MOF for enhanced catalytic activity under extreme conditions |
title | Translocation of enzymes into a mesoporous MOF for enhanced catalytic activity under extreme conditions
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title_full | Translocation of enzymes into a mesoporous MOF for enhanced catalytic activity under extreme conditions
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title_fullStr | Translocation of enzymes into a mesoporous MOF for enhanced catalytic activity under extreme conditions
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title_full_unstemmed | Translocation of enzymes into a mesoporous MOF for enhanced catalytic activity under extreme conditions
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title_short | Translocation of enzymes into a mesoporous MOF for enhanced catalytic activity under extreme conditions
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title_sort | translocation of enzymes into a mesoporous mof for enhanced catalytic activity under extreme conditions |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6469195/ https://www.ncbi.nlm.nih.gov/pubmed/31049190 http://dx.doi.org/10.1039/c9sc00082h |
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