Magnetic nanoparticles coated with polyaniline to stabilize immobilized trypsin

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• 作者：J. C. Maciel ; A. A. D. Mercês ; M. Cabrera ; W. T. Shigeyosi…
• 关键词：Magnetic nanoparticles ; PANI ; Trypsin ; Biomedical applications
• 刊名：Hyperfine Interactions
• 出版年：2016
• 出版时间：December 2016
• 年：2016
• 卷：237
• 期：1
• 全文大小：1,520 KB
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• 作者单位：J. C. Maciel (1)
  A. A. D. Mercês (2)
  M. Cabrera (2)
  W. T. Shigeyosi (3)
  S. D. de Souza (4)
  M. Olzon-Dionysio (4)
  J. D. Fabris (4)
  C. A. Cardoso (3)
  D. F. M. Neri (5)
  M. P. C. Silva (2)
  L. B. Carvalho Jr. (2)
  
  1. Universidade Federal de Roraima, Campus Paricarana, 69301–000, Boa Vista, Roraima, Brazil
  2. Laboratório de Imunopatologia Keizo Asami, Universidade Federal de Pernambuco, Recife, PE, Brazil
  3. Departamento de Física, Universidade Federal de São Carlos, São Carlos, SP, Brazil
  4. Universidade Federal dos Vales de Jequitinhonha e Mucuri, Diamantina, MG, Brazil
  5. Universidade Federal do Vale do São Francisco, Petrolina, PE, Brazil
  
• 刊物类别：Physics and Astronomy
• 刊物主题：Physics
  Nuclear Physics, Heavy Ions and Hadrons
  Atoms, Molecules, Clusters and Plasmas
  Condensed Matter
  Surfaces and Interfaces and Thin Films
  
• 出版者：Springer Netherlands
• ISSN：1572-9540

文摘

It is reported the synthesis of magnetic nanoparticles via the chemical co-precipitation of Fe 3+ ions and their preparation by coating them with polyaniline. The electronic micrograph analysis showed that the mean diameter for the nanoparticles is ∼15 nm. FTIR, powder X-ray diffraction and Mössbauer spectroscopy were used to understand the chemical, crystallographic and 57Fe hyperfine structures for the two samples. The nanoparticles, which exhibited magnetic behavior with relatively high spontaneous magnetization at room temperature, were identified as being mainly formed by maghemite (γFe₂O₃). The coated magnetic nanoparticles (sample labeled “mPANI”) presented a real ability to bind biological molecules such as trypsin, forming the magnetic enzyme derivative (sample “mPANIG-Trypsin”). The amount of protein and specific activity of the immobilized trypsin were found to be 13±5 μg of protein/mg of mPANI (49.3 % of immobilized protein) and 24.1±0.7 U/mg of immobilized protein, respectively. After 48 days of storage at 4 ∘C, the activity of the immobilized trypsin was found to be 89 % of its initial activity. This simple, fast and low-cost procedure was revealed to be a promising way to prepare mPANI nanoparticles if technological applications addressed to covalently link biomolecules are envisaged. This route yields chemically stable derivatives, which can be easily recovered from the reaction mixture with a magnetic field and recyclable reused.