Abstract
Enzymatic amperometric procedures for measuring arsenic, based on the inhibitive action of this metal on acetylcholinesterase enzyme activity, have been developed. Screen-printed carbon electrodes (SPCEs) were used with acetylcholinesterase covalently bonded directly to its surface. The amperometric response of acetylcholinesterase was affected by the presence of arsenic ions, which caused a decrease in the current intensity. The experimental optimum working conditions of pH, substrate concentration and potential applied, were established. Under these conditions, repeatability and reproducibility of biosensors were determined, reaching values below 4% in terms of relative standard deviation. The detection limit obtained for arsenic was 1.1 × 10−8 M for Ach/SPCE biosensor. Analysis of the possible effect of the presence of foreign ions in the solution was performed. The method was applied to determine levels of arsenic in spiked tap water samples.
Highlights
Nowadays, environmental pollution caused by metals in different quantities is common, and their traces may often originate from natural as well as anthropogenic sources
The enzyme was immobilized by covalent linkage on the surface of screen-printed carbon electrodes (SPCEs)
In order to build the Ach/SPE biosensor, several experiments were done with the aim to find the optimum conditions for enzyme immobilization
Summary
Environmental pollution caused by metals in different quantities is common, and their traces may often originate from natural as well as anthropogenic sources. Electroanalytical techniques bring with them important advantages, such as high sensitivity, low detection limits, relative simplicity, low costs and portable field-based equipment able to determine trace elements. For this reason, electrochemical techniques offer an interesting alternative to methods that are currently in use. Voltammetric methods are among the electrochemical techniques described for the analysis of arsenic These are relatively widespread, and due to their accuracy and sensitivity, have contributed greatly to its determination at trace level [8,9]. The enzyme was immobilized by covalent linkage on the surface of screen-printed carbon electrodes (SPCEs)
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
