Temperature-Switchable Agglomeration of Magnetic Particles Designed for Continuous Separation Processes in Biotechnology
| Autor: | Matthias Franzreb, Huey Wen Ooi, Raphael Heinzler, Anja Paulus |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Ammonium sulfate
Thermogravimetric analysis Kosmotropic Materials science Economies of agglomeration Acrylic Resins Temperature Proteins Microspheres chemistry.chemical_compound chemistry Chemical engineering Polymerization Polymer chemistry Poly(N-isopropylacrylamide) Magnetic nanoparticles Particle General Materials Science Magnetite Nanoparticles Biotechnology Protein Binding |
| Zdroj: | ACS applied materialsinterfaces. 7(26) |
| ISSN: | 1944-8252 |
| Popis: | The purpose of this work was the synthesis and characterization of thermally switchable magnetic particles for use in biotechnological applications such as protein purification and enzymatic conversions. Reversible addition-fragmentation chain-transfer polymerization was employed to synthesize poly(N-isopropylacrylamide) brushes via a "graft-from" approach on the surface of magnetic microparticles. The resulting particles were characterized by infrared spectroscopy and thermogravimetric analysis and their temperature-dependent agglomeration behavior was assessed. The influence of several factors on particle agglomeration (pH, temperature, salt type, and particle concentration) was evaluated. The results showed that a low pH value (pH 3-4), a kosmotropic salt (ammonium sulfate), and a high particle concentration (4 g/L) resulted in improved agglomeration at elevated temperature (40 °C). Recycling of particles and reversibility of the temperature-switchable agglomeration were successfully demonstrated for ten heating-cooling cycles. Additionally, enhanced magnetic separation was observed for the modified particles. Ionic monomers were integrated into the polymer chain to create end-group functionalized particles as well as two- and three-block copolymer particles for protein binding. The adsorption of lactoferrin, bovine serum albumin, and lysozyme to these ion exchange particles was evaluated and showed a binding capacity of up to 135 mg/g. The dual-responsive particles combined magnetic and thermoresponsive properties for switchable agglomeration, easy separability, and efficient protein adsorption. |
| Databáze: | OpenAIRE |
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