ArticleLangmuir : the ACS journal of surfaces and colloids2022
Enzyme Immobilization on Metal Organic Frameworks: the Effect of Buffer on the Stability of the Support.
Article in Langmuir : the ACS journal of surfaces and colloids, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 46 citations in OpenAlex.
- Quantitative design principles for biofunctional metal-organic frameworks: Stability thresholds, biointerface energetics, and therapeutic applications.Materials today. Bio · 2026Review
- Review
- Synthesis and characterization of ZrFeNanoscale advances · 2026Article
- Acid-Responsive Zeolitic Imidazolate Framework-8 Core-Shell Nanovesicles Loaded with Interleukin-2 Nanoplatforms Selectively Expand Regulatory T Cells to Reconstruct Immunometabolic Homeostasis in Diabetic Neuropathy.Biomaterials research · 2026Article
- Reticular Frameworks for Advanced Polymer Materials.Advanced materials (Deerfield Beach, Fla.) · 2026Review
- Introducing metal-sulfur active sites in metal-organic frameworks via post-synthetic modification for hydrogenation catalysis.Nature chemistry · 2025Article
- Tailored Metal-Organic Framework-Based Enzyme Hybrids: Immobilization Strategies, Improved Performance, and Biological Applications.Small science · 2025Review
- Catalysis in Chemical Modification of Proteins.ChemCatChem · 2025Article
- Closing the Loop in the Carbon Cycle: Enzymatic Reactions Housed in Metal-Organic Frameworks for COApplied biochemistry and biotechnology · 2025Review
- Review
- Metal-Organic Frameworks: Versatile Platforms for Biomedical Innovations.Materials (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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