Supramolecular assembly of L-Lysine on ZSM-5 zeolites with different Si/Al ratio
| Autor: | Matteo Ardit, Lara Gigli, Massimo Migliori, Luisa Pasti, Giada Beltrami, Girolamo Giordano, Giulia Vergine, Enrico Catizzone, Mirco Cescon, Tatiana Chenet, Annalisa Martucci |
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| Přispěvatelé: | Chenet, T., Martucci, A., Cescon, M., Vergine, G., Beltrami, G., Gigli, L., Ardit, M., Migliori, M., Catizzone, E., Giordano, G., Pasti, L. |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Supramolecular chemistry
02 engineering and technology 010402 general chemistry complex mixtures 01 natural sciences Supramolecular assembly Adsorption Molecule General Materials Science Self-assembly process Equilibrium constant Zeolite Chemistry Amino acids Zeolite Self-assembly process Adsorption Intermolecular force Ambientale General Chemistry 021001 nanoscience & nanotechnology Condensed Matter Physics Binding constant 0104 chemical sciences Crystallography Mechanics of Materials bacteria Amino acids ZSM-5 0210 nano-technology |
| Popis: | The adsorption of the amino acid, l -lysine, on two ZSM-5 having different silicon to aluminium ratio (i.e. Si/Al = 15 and 37) has been investigated by experiments at macroscopic and at atomistic level resolution. The kinetic and equilibrium constants of the adsorption processes obtained for both the adsorption materials, show that Al content is an important factor in tuning the adsorption of the amino acid on the zeolite. Both the saturation capacity and the binding constant decrease as Si/Al ratio increases. The refinements of high resolution X-ray diffraction data obtained from synchrotron radiation, indicate that adsorption of l -lysine in ZSM-5 is a surface-confined supramolecular self-assembly process. l -lysine molecules at the intersection of the sinusoidal and the straight channels, are arranged in a α-helical conformation stabilized by the simultaneous occurrence of strong H-bonds among the tail of l -lysine molecules, water molecules and framework oxygens. l -lysine molecules within the sinusoidal channel are arranged as β-sheets forming infinite hydrogen-bonding β-strands with the framework oxygens. Our results suggest that l -lysine conformation strongly depends on both pH and hydration state influencing amino acids physico-chemical properties and intermolecular bond energies. |
| Databáze: | OpenAIRE |
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