Sharif Digital Repository

A manganese porphyrin, meso-tetrakis(pentafluorophenyl)porphyrinato manganese(iii) acetate, Mn(TPFPP)OAc, was immobilized on silica-coated magnetic Fe3O4 nanoparticles functionalized with 3-aminopropyltriethoxysilane (APTS) through the amino propyl linkage using a grafting process in toluene solvent. This enabled the covalent immobilization of Mn(iii) porphyrin via an aromatic nucleophilic substitution reaction, to afford the Fe3O4@SiO2-NH2@MnPor catalyst. The resulting nanoparticles were characterized by X-ray powder diffraction (XRD), scanning electron microscopy (SEM), FT-IR spectroscopy, UV-Vis spectroscopy, elemental analysis (CHN), atomic absorption spectroscopy (AAS), and vibrating... 

Graphene-based materials are revealing the leading edge of advanced technology for their exceptional physical and chemical properties. Chemical manipulation on graphene surface to tailor its unique properties and modify atomic structures is being actively pursued. Therefore, the discovery of robust and general protocols to anchor active functionality on graphene basal plane is still of great interest. Multicomponent reactions promise an enormous level of interest due to addressing both diversity and complexity in combinatorial synthesis, in which more than two starting compounds react to form a product derived from entire inputs. In this article, we present the first covalent... 

A magnetic nanocomposite was prepared by entrapment of Fe3O4 nanoparticles into the cross-linked ionic liquid/epoxy type polymer. The resulting support was used for covalent immobilization of cellulase through the reaction with epoxy groups. The ionic surface of the support improved the adsorption of enzyme, and a large amount of enzyme (106.1 mg/g) was loaded onto the support surface. The effect of the presence of ionic monomer and covalent binding of enzyme was also investigated. The structure of support was characterized by various instruments such as FT-IR, TGA, VSM, XRD, TEM, SEM, and DLS. The activity and stability of immobilized cellulase were investigated in the prepared support. The... 

In this study, graphene oxide (GO) was synthesized via modified Hummer's method and exploited as an ideal enzyme immobilization support due to its exclusive chemical and structural features. Then, laccase from genetically modified Aspergillus was covalently immobilized onto GO (nanobiocatalyst). Enzymatic characterization of the nanobiocatalyst exhibited promising results: laccase loading of 156.5 mg g−1 and immobilization yield of 64.6% at laccase concentration of 0.9 mg/ mL. Further employment of various structural characterization techniques including Fourier Transform Infrared Spectroscopy (FTIR), X-ray Powder Diffraction (XRD), Scanning Electron Microscopy (SEM), Thermo-Gravimetric...