Next Article in Journal
Special Issue: Intramolecular Hydrogen Bonding
Next Article in Special Issue
Substrate Specificity and Enzyme Recycling Using Chitosan Immobilized Laccase
Previous Article in Journal
Design, Synthesis and SAR Studies of NAD Analogues as Potent Inhibitors towards CD38 NADase
Previous Article in Special Issue
Carbon Nanotubes as Supports for Inulinase Immobilization
Article Menu
Issue 10 (October) cover image

Export Article

Open AccessArticle
Molecules 2014, 19(10), 15768-15782; doi:10.3390/molecules191015768

Immobilization of Horseradish Peroxidase on NH2-Modified Magnetic Fe3O4/SiO2 Particles and Its Application in Removal of 2,4-Dichlorophenol

Key Laboratory of Catalysis and Materials Science of the State Ethnic Affairs Commission and Ministry of Education, College of Chemistry and Materials Science, South-Central University for Nationalities, Wuhan 430074, China
*
Author to whom correspondence should be addressed.
Received: 14 May 2014 / Revised: 9 August 2014 / Accepted: 7 September 2014 / Published: 29 September 2014
(This article belongs to the Special Issue Enzyme Immobilization)
View Full-Text   |   Download PDF [1766 KB, uploaded 29 September 2014]   |  

Abstract

Fe3O4 nanoparticles were prepared by a co-precipitation method with the assistance of ultrasound irradiation, and then coated with silica generated by hydrolysis and condensation of tetraethoxysilane. The silica-coated Fe3O4 nanoparticles were further modified with 3-aminopropyltriethoxysilane, resulting in anchoring of primary amine groups on the surface of the particles. Horseradish peroxidase (HRP) was then immobilized on the magnetic core-shell particles by using glutaraldehyde as a crosslinking agent. Immobilization conditions were optimized to obtain the highest relative activity of the immobilized enzyme. It was found the durability of the immobilized enzyme to heating and pH variation were improved in comparison with free HRP. The apparent Michaelis constants of the immobilized HRP and free HRP with substrate were compared, showing that the enzyme activity of the immobilized HRP was close to that of free HRP. The HRP immobilized particles, as an enzyme catalyst, were used to activate H2O2 for degrading 2,4-dichlorophenol. The rapid degradation of 2,4-dichlorophenol indicated that the immobilized enzyme has potential applications for removing organic pollutants. View Full-Text
Keywords: magnetite nanoparticles; silica; immobilized enzyme; horseradish peroxidase; degradation; 2,4-dichlorophenol magnetite nanoparticles; silica; immobilized enzyme; horseradish peroxidase; degradation; 2,4-dichlorophenol
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Chang, Q.; Tang, H. Immobilization of Horseradish Peroxidase on NH2-Modified Magnetic Fe3O4/SiO2 Particles and Its Application in Removal of 2,4-Dichlorophenol. Molecules 2014, 19, 15768-15782.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top