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Screen-printed electrodes modified with HRP-zirconium alcoxide film for the development of a biosensor for acetaminophen detection

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Sima V., Cristea C., Bodoki E., Duţu G., Sāndulescu R.
Open Chemistry
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2010
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vol. 8
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issue 5
1034-1040
EN
The development of a biosensor based on the immobilization of horseradish peroxidase (HRP) within a zirconium alkoxide-polyetilenimine film onto screen-printed electrodes (SPE) for acetaminophen detection and acetaminophen quantification in pharmaceutical products is described. The biosensor operation mode is based on monitoring the amperometric signal produced by the electrochemical reduction of the enzymatically generated electroactive oxidized species of acetaminophen in the presence of hydrogen peroxide. The enzyme immobilization is performed by retention in a polyethylenimine-zirconium alcoxide porous gel film, a technique that offers good entrapping and a protective environment for the biocomponent due to the hydration properties of the immobilization layer. SPEs have the advantage of being easily mass-produced at low costs with superior characteristics in comparison with classical electrode materials. In this configuration, zirconium alkoxide demonstrates its electrocatalytic activity. The biosensor allows the quantification of acetaminophen with a limit of detection of 6.21×10−8 M and a linear range between 4.35×10−7 M and 4.98×10−6 M. Finally, the biosensor is applied to the quantitative analysis of acetaminophen in Perdolan® tablets. [...]
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Stabilization of horseradish peroxidase by covalent conjugation with dextran aldehyde against temperature and pH changes

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Altikatoglu M., Arioz C., Basaran Y., Kuzu H.
Open Chemistry
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2009
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vol. 7
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issue 3
423-428
EN
Stabilization of Horseradish Peroxidase (HRP; EC 1.11.1.7) against temperature and pH via the formation of the conjugates obtained by multipoint covalent bonding of dextran aldehyde (DA) to the enzyme were studied. Hence, three different molar weighted dextrans (17.5 kD, 75 kD, 188 kD) were covalently bonded to purified enzyme with different molar ratios (nHRP/nDA 20/1, 10/1, 1/1, 1/5, 1/10, 1/15, 1/20). The thermal stabilities of the obtained conjugates were evaluated with the activities determined at different temperatures (25, 30, 35, 40, 50, 60, 70, 80°C) applying 60 minutes incubation time. Conjugates formed were characterized by gel-permeation chromatography (GPC) and fluorescence techniques. The conjugate synthesized using dextran 75 kDa with nHRP/nDA 1/10 molar ratio showed better thermal stability than other conjugates and purified enzyme at pH 7. This conjugate also has wider activity pH range than purified enzyme. In addition, mentioned conjugate at pH 7 had very long storage lifetime compared to purified enzyme at +4°C and room temperature; which is considered a favorable feature for usage in practice. [...]
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