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Study of Enzyme (Chymotrypsin) -Core/Shell (Fe3O4 @ Au) Nanoparticle Bioconjugate

Kamal Ahmadi, Mahmoud | 2011

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  1. Type of Document: M.Sc. Thesis
  2. Language: Farsi
  3. Document No: 41826 (06)
  4. University: Sharif University of Technology
  5. Department: Chemical and Petroleum Engineering
  6. Advisor(s): Vosoughi, Manoochehr; Seyf Kordi, Ali Akbar
  7. Abstract:
  8. Conjugation of proteins to nanoparticles has numerous applications in sensing, imaging, delivery, catalysis, therapy and control of protein structure and activity. Therefore, characterizing the nanoparticle–protein interface is of great importance. A variety of covalent and non-covalent linking chemistries have been reported for nanoparticle attachment. Typically, a specific protein residue is linked directly to the nanoparticle core or to the ligand. As conjugation often affects the protein structure and function, techniques to probe structure and activity are assessed Characterization studies of nanoparticle–protein complexes show that the structure and function are influenced by the chemistry of the nanoparticle ligand, the nanoparticle size, the nanoparticle material, the stochiometry of the conjugates, the labeling site on the protein and the nature of the linkage (covalent versus non-covalent). In this Project we examined attachment of an Enzyme (Chymotrypsin) on the surface of ferrous magnetite oxide/ Au core/shell. The resulted structure carefully characterized using FTIR, XRD, SEM and Fluorescence Spectroscopy. In addition, activity of immobilized enzyme was determined via casein assay and was compared with data of free enzyme. Our investigation shows the third and second structure of protein remain almost unchanged during immobilization. While, activity of enzyme reduced by thirty percent
  9. Keywords:
  10. Enzyme Stabilization ; Ferrite-Gold Nanoparticle ; Core-Shell Nanostructure ; Protein Structure ; Chymotrypsin Enzyme ; Enzyme Activity

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