Volume 6, Issue 1 (12-2018)
J Environ Health Eng 2018, 6(1): 111-124 |
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Razmi E, Jonidi Jafari A, Esrafili A, Dehghanifard E, Rezaei Kalantari R. Immobilization of Laccase Enzyme on Silica-Coated Iron Oxide Nanoparticles and Comparison of Stability and Activity of Free and Immobilized Laccase. J Environ Health Eng 2018; 6 (1) :111-124
URL: http://jehe.abzums.ac.ir/article-1-581-en.html
URL: http://jehe.abzums.ac.ir/article-1-581-en.html
Department of Environmental Health Engineering, School of Public Health, Iran University of Medical Sciences, Tehran, Iran
Abstract: (2627 Views)
Background: Laccase enzyme is capable of oxidizing many resistant and non-biodegradable
environmental pollutants, so it has been studied frequently in recent years and is widely used in
biodegradation of contaminants. Despite its abundant applicability, due to its short life span, nonrecovery,
thermal instability and instability in organic environments, its widespread use is very limited.
The present study aimed to increase the stability of laccase by immobilizing it on silica coated iron
oxide nanoparticles.
Materials and Methods: Fe3O4 nanoparticles were synthesized based on the co-precipitation
method and after coating with silica, their surface was modified by amine groups. The enzyme was
then immobilized by covalent binding using glutaraldehyde. Specifications of synthesized
nanoparticles and immobilized enzyme were investigated using X-ray diffraction (XRD), Field
Emission Scanning Electron Microscopy (FESEM), and Energy-dispersive X-ray spectroscopy
(EDX).
Results: Results of successful laccase immobilization on nanoparticles showed that laccase
immobilization significantly increased storage and thermal stability, maintaining activity in a wider
range of temperature and pH than free laccase.
Conclusion: The immobilization of laccase on silica-coated iron oxide nanoparticles can reduce the
barriers and challenges of various enzymes by increasing its efficiency and stability.
environmental pollutants, so it has been studied frequently in recent years and is widely used in
biodegradation of contaminants. Despite its abundant applicability, due to its short life span, nonrecovery,
thermal instability and instability in organic environments, its widespread use is very limited.
The present study aimed to increase the stability of laccase by immobilizing it on silica coated iron
oxide nanoparticles.
Materials and Methods: Fe3O4 nanoparticles were synthesized based on the co-precipitation
method and after coating with silica, their surface was modified by amine groups. The enzyme was
then immobilized by covalent binding using glutaraldehyde. Specifications of synthesized
nanoparticles and immobilized enzyme were investigated using X-ray diffraction (XRD), Field
Emission Scanning Electron Microscopy (FESEM), and Energy-dispersive X-ray spectroscopy
(EDX).
Results: Results of successful laccase immobilization on nanoparticles showed that laccase
immobilization significantly increased storage and thermal stability, maintaining activity in a wider
range of temperature and pH than free laccase.
Conclusion: The immobilization of laccase on silica-coated iron oxide nanoparticles can reduce the
barriers and challenges of various enzymes by increasing its efficiency and stability.
Type of Study: Research |
Subject:
Special
Received: 2018/12/30 | Accepted: 2018/12/30 | Published: 2018/12/30
Received: 2018/12/30 | Accepted: 2018/12/30 | Published: 2018/12/30
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