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Synthesis of Magnetic Gold Mesoporous Silica Nanoparticles Core Shell for Cellulase Enzyme Immobilization: Improvement of Enzymatic Activity and Thermal Stability Publisher



Poorakbar E1, 2, 3 ; Shafiee A2 ; Saboury AA3 ; Rad BL1 ; Khoshnevisan K4 ; Mamani L5 ; Derakhshankhah H6 ; Ganjali MR7 ; Hosseini M8
Authors
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Authors Affiliations
  1. 1. Department of Biology, Faculty of Sciences, Payame Noor University, P.O.Box: 19395-3697, Tehran, Iran
  2. 2. Department of Pharmaceutics, Tehran University of Medical Science, Tehran, Iran
  3. 3. Institute of Biophysics and Biochemistry, University of Tehran, Tehran, Iran
  4. 4. Biosensor Research Center, Endocrinology and Metabolism Molecular-Cellular Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran
  5. 5. Department of Nanotechnology, Agricultural Biotechnology Research Institute of Iran (ABRII), Karaj, Iran
  6. 6. Pharmacutical Sciences Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran
  7. 7. Center of Excellence in Electrochemistry, Faculty of Chemistry, University of Tehran, Tehran, Iran
  8. 8. Department of Life Science Engineering, Faculty of New Sciences & Technologies, University of Tehran, Tehran, Iran

Source: Process Biochemistry Published:2018


Abstract

Magnetic gold mesoporous silica nanoparticle core shells (mAu@PSNs) were fabricated as a support and their size, morphology and structure was further characterized by X-Ray diffraction (XRD), vibrating sample magnetometer (VSM), scanning electron microscopy (SEM), energy dispersive X-ray analysis (EDAX), transmission electron microscopy (TEM), dynamic light scattering (DLS) and thermal gravimetric analysis (TGA). Cellulase (CEL) immobilization on mAu@PSNs was performed via covalent bonding. Fourier transform infrared (FTIR) spectroscopy confirmed the successful binding of enzyme to mAu@PSNs while Bradford assay determined the binding efficiency to be 76%. The enzyme activity was measured at different pHs and temperatures by FPase method using Whatman filter paper as the substrate. The immobilized enzyme maintained 58% of its initial catalytic activity after nine hours. In this research, a new nano-system was designed as a solid support for cellulase immobilization which enhanced its thermal stability and facilitated its long term storage. In addition, the immobilized enzyme can be applied in a broader temperature and pH ranges while enzyme separation can be simply carried out by an external magnet. © 2018 Elsevier Ltd