A phenol biosensor based on immobilizing tyrosinase to modified core-shell magnetic nanoparticles supported at a carbon paste electrode [An article from: Analytica Chimica Acta]
Book Details
PublisherElsevier
ISBN / ASINB000RR3H6A
ISBN-13978B000RR3H65
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Description
This digital document is a journal article from Analytica Chimica Acta, published by Elsevier in 2005. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.
Description:
A phenol biosensor was developed based on the immobilization of tyrosinase on the surface of modified magnetic MgFe"2O"4 nanoparticles. The tyrosinase was first covalently immobilized to core-shell (MgFe"2O"4-SiO"2) magnetic nanoparticles, which were modified with amino group on its surface. The resulting magnetic bio-nanoparticles were attached to the surface of carbon paste electrode (CPE) with the help of a permanent magnet. The immobilization matrix provided a good microenvironment for the retaining of the bioactivity of tyrosinase. Phenol was determined by the direct reduction of biocatalytically generated quinone species at -150mV versus SCE. The resulting phenol biosensor could reach 95% of steady-state current within 20s and exhibited a high sensitivity of 54.2@mA/mM, which resulted from the high tyrosinase loading of the immobilization matrix. The linear range for phenol determination was from 1x10^-^6 to 2.5x10^-^4M with a detection limit of 6.0x10^-^7M obtained at a signal-to-noise ratio of 3. The stability and the application of the biosensor were also evaluated.
Description:
A phenol biosensor was developed based on the immobilization of tyrosinase on the surface of modified magnetic MgFe"2O"4 nanoparticles. The tyrosinase was first covalently immobilized to core-shell (MgFe"2O"4-SiO"2) magnetic nanoparticles, which were modified with amino group on its surface. The resulting magnetic bio-nanoparticles were attached to the surface of carbon paste electrode (CPE) with the help of a permanent magnet. The immobilization matrix provided a good microenvironment for the retaining of the bioactivity of tyrosinase. Phenol was determined by the direct reduction of biocatalytically generated quinone species at -150mV versus SCE. The resulting phenol biosensor could reach 95% of steady-state current within 20s and exhibited a high sensitivity of 54.2@mA/mM, which resulted from the high tyrosinase loading of the immobilization matrix. The linear range for phenol determination was from 1x10^-^6 to 2.5x10^-^4M with a detection limit of 6.0x10^-^7M obtained at a signal-to-noise ratio of 3. The stability and the application of the biosensor were also evaluated.
