Cargando…

Enzyme Immobilization on Metal Organic Frameworks: the Effect of Buffer on the Stability of the Support

[Image: see text] Metal organic frameworks (MOFs) have been used to encapsulate an array of enzymes in a rapid and facile manner; however, the stability of MOFs as supports for enzymes has not been examined in detail. This study examines the stability of MOFs with different compositions (Fe-BTC, Co-...

Descripción completa

Detalles Bibliográficos
Autores principales: Shortall, Kim, Otero, Fernando, Bendl, Simon, Soulimane, Tewfik, Magner, Edmond
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9648341/
https://www.ncbi.nlm.nih.gov/pubmed/36286410
http://dx.doi.org/10.1021/acs.langmuir.2c01630
_version_ 1784827561298100224
author Shortall, Kim
Otero, Fernando
Bendl, Simon
Soulimane, Tewfik
Magner, Edmond
author_facet Shortall, Kim
Otero, Fernando
Bendl, Simon
Soulimane, Tewfik
Magner, Edmond
author_sort Shortall, Kim
collection PubMed
description [Image: see text] Metal organic frameworks (MOFs) have been used to encapsulate an array of enzymes in a rapid and facile manner; however, the stability of MOFs as supports for enzymes has not been examined in detail. This study examines the stability of MOFs with different compositions (Fe-BTC, Co-TMA, Ni-TMA, Cu-TMA, and ZIF-zni) in buffered solutions commonly used in enzyme immobilization and biocatalysis. Stability was assessed via quantification of the release of metals by inductively coupled plasma optical emission spectroscopy. The buffers used had varied effects on different MOF supports, with incubation of all MOFs in buffers resulting in the release of metal ions to varying extents. Fe-BTC was completely dissolved in citrate, a buffer that has a profound destabilizing effect on all MOFs analyzed, precluding its use with MOFs. MOFs were more stable in acetate, potassium phosphate, and Tris HCl buffers. The results obtained provide a guide for the selection of an appropriate buffer with a particular MOF as a support for the immobilization of an enzyme. In addition, these results identify the requirement to develop methods of improving the stability of MOFs in aqueous solutions. The use of polymer coatings was evaluated with polyacrylic acid (PAA) providing an improved level of stability. Lipase was immobilized in Fe-BTC with PAA coating, resulting in a stable biocatalyst with retention of activity in comparison to the free enzyme.
format Online
Article
Text
id pubmed-9648341
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher American Chemical Society
record_format MEDLINE/PubMed
spelling pubmed-96483412022-11-15 Enzyme Immobilization on Metal Organic Frameworks: the Effect of Buffer on the Stability of the Support Shortall, Kim Otero, Fernando Bendl, Simon Soulimane, Tewfik Magner, Edmond Langmuir [Image: see text] Metal organic frameworks (MOFs) have been used to encapsulate an array of enzymes in a rapid and facile manner; however, the stability of MOFs as supports for enzymes has not been examined in detail. This study examines the stability of MOFs with different compositions (Fe-BTC, Co-TMA, Ni-TMA, Cu-TMA, and ZIF-zni) in buffered solutions commonly used in enzyme immobilization and biocatalysis. Stability was assessed via quantification of the release of metals by inductively coupled plasma optical emission spectroscopy. The buffers used had varied effects on different MOF supports, with incubation of all MOFs in buffers resulting in the release of metal ions to varying extents. Fe-BTC was completely dissolved in citrate, a buffer that has a profound destabilizing effect on all MOFs analyzed, precluding its use with MOFs. MOFs were more stable in acetate, potassium phosphate, and Tris HCl buffers. The results obtained provide a guide for the selection of an appropriate buffer with a particular MOF as a support for the immobilization of an enzyme. In addition, these results identify the requirement to develop methods of improving the stability of MOFs in aqueous solutions. The use of polymer coatings was evaluated with polyacrylic acid (PAA) providing an improved level of stability. Lipase was immobilized in Fe-BTC with PAA coating, resulting in a stable biocatalyst with retention of activity in comparison to the free enzyme. American Chemical Society 2022-10-26 2022-11-08 /pmc/articles/PMC9648341/ /pubmed/36286410 http://dx.doi.org/10.1021/acs.langmuir.2c01630 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Shortall, Kim
Otero, Fernando
Bendl, Simon
Soulimane, Tewfik
Magner, Edmond
Enzyme Immobilization on Metal Organic Frameworks: the Effect of Buffer on the Stability of the Support
title Enzyme Immobilization on Metal Organic Frameworks: the Effect of Buffer on the Stability of the Support
title_full Enzyme Immobilization on Metal Organic Frameworks: the Effect of Buffer on the Stability of the Support
title_fullStr Enzyme Immobilization on Metal Organic Frameworks: the Effect of Buffer on the Stability of the Support
title_full_unstemmed Enzyme Immobilization on Metal Organic Frameworks: the Effect of Buffer on the Stability of the Support
title_short Enzyme Immobilization on Metal Organic Frameworks: the Effect of Buffer on the Stability of the Support
title_sort enzyme immobilization on metal organic frameworks: the effect of buffer on the stability of the support
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9648341/
https://www.ncbi.nlm.nih.gov/pubmed/36286410
http://dx.doi.org/10.1021/acs.langmuir.2c01630
work_keys_str_mv AT shortallkim enzymeimmobilizationonmetalorganicframeworkstheeffectofbufferonthestabilityofthesupport
AT oterofernando enzymeimmobilizationonmetalorganicframeworkstheeffectofbufferonthestabilityofthesupport
AT bendlsimon enzymeimmobilizationonmetalorganicframeworkstheeffectofbufferonthestabilityofthesupport
AT soulimanetewfik enzymeimmobilizationonmetalorganicframeworkstheeffectofbufferonthestabilityofthesupport
AT magneredmond enzymeimmobilizationonmetalorganicframeworkstheeffectofbufferonthestabilityofthesupport