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Buffer Effects in Zirconium-Based UiO Metal-Organic Frameworks (MOFs) That Influence Enzyme Immobilization and Catalytic Activity in Enzyme/MOF Biocatalysts.
| Content Provider | Europe PMC |
|---|---|
| Author | Ahmad, Raneem Rizaldo, Sydnie Gohari, Mahnaz Shanahan, Jordan Shaner, Sarah E. Stone, Kari L. Kissel, Daniel S. |
| Copyright Year | 2023 |
| Abstract | Novel biocatalyststhat feature enzymes immobilized onto solidsupports have recently become a major research focus in an effortto create more sustainable and greener chemistries in catalysis. Manyof these novel biocatalyst systems feature enzymes immobilized ontometal–organic frameworks (MOFs), which have been shown to increaseenzyme activity, stability, and recyclability in industrial processes.While the strategies used for immobilizing enzymes onto MOFs can vary,the conditions always require a buffer to maintain the functionalityof the enzymes during immobilization. This report brings attentionto critical buffer effects important to consider when developing enzyme/MOFbiocatalysts, specifically for buffering systems containing phosphateions. A comparative analysis of different enzyme/MOF biocatalystsfeaturing horseradish peroxidase and/or glucose oxidase immobilizedonto the MOFs UiO-66, UiO-66-NH2, and UiO-67 using a noncoordinatebuffering system (MOPSO buffer) and a phosphate buffering system (PBS)show that phosphate ions can have an inhibitory effect. Previous studiesutilizing phosphate buffers for enzyme immobilization onto MOFs haveshown Fourier transform infrared (FT-IR) spectra that have been assignedstretching frequencies associated with enzymes after immobilization.Analyses and characterizations using zeta potential measurements,scanning electron microscopy, Brunauer–Emmett–Tellersurface area, powder X-ray diffraction, Energy Dispersive X-ray Spectroscopy,and FT-IR show concerning differences in enzyme loading and activitybased on the buffering system used during immobilization. |
| Journal | ACS Omega |
| Volume Number | 8 |
| PubMed Central reference number | PMC10308582 |
| Issue Number | 25 |
| PubMed reference number | 37396281 |
| e-ISSN | 24701343 |
| DOI | 10.1021/acsomega.3c00703 |
| Language | English |
| Publisher | American Chemical Society |
| Publisher Date | 2023-06-09 |
| Access Restriction | Open |
| Rights License | Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). © 2023 The Authors. Published by American Chemical Society |
| Content Type | Text |
| Resource Type | Article |
| Subject | Chemistry Chemical Engineering |
