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Creating magnetic ionic liquid-molecularly imprinted polymers for selective extraction of lysozyme
A novel magnetic (Fe(3)O(4)) surface molecularly imprinted polymer (MIP) based on ionic liquid (IL) (Fe(3)O(4)@VTEO@IL-MIPs) was prepared for the selective extraction of lysozyme (Lys). As the functional monomer of the MIPs, an imidazolium-based IL with vinyl groups was prepared. It can provide mult...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9081177/ https://www.ncbi.nlm.nih.gov/pubmed/35541737 http://dx.doi.org/10.1039/c8ra03818j |
Sumario: | A novel magnetic (Fe(3)O(4)) surface molecularly imprinted polymer (MIP) based on ionic liquid (IL) (Fe(3)O(4)@VTEO@IL-MIPs) was prepared for the selective extraction of lysozyme (Lys). As the functional monomer of the MIPs, an imidazolium-based IL with vinyl groups was prepared. It can provide multiple interactions with template molecules. The amount of IL was optimized (200 mg). Fourier transform infrared spectrometry (FT-IR), transmission electron microscopy (TEM), dynamic light scattering (DLS), thermogravimetric analysis (TGA) and a vibrating sample magnetometer (VSM) were used to characterize the MIP. The results indicate the successful formation of an imprinting polymer layer. The concentration of Lys in the supernatant was determined by UV-vis spectrophotometry at a wavelength of 280 nm. The maximum adsorption capability of the MIP is 213.7 mg g(−1) and the imprinting factor (IF) is 2.02. It took 2.5 h for the MIP to attain adsorption equilibrium. The structure of the protein was evaluated using circular dichroism (CD) spectra and UV-visible spectra. The adsorption performance was further investigated in detail by selective adsorption experiments, competitive rebinding tests, and reusability and stability experiments. Furthermore, it was utilized to separate the template protein from a mixture of proteins and real samples successfully because of the high adsorption capacity for Lys. |
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