Detection of pesticide by polymeric enzyme electrodes.

Screen-printed electrodes (SPEs) containing immobilized acetylcholine esterase (AChE) enzyme were used for the electrochemical determination of organophosphorous (OP) and carbamate pesticides. The extent of AChE deactivation by the pesticide was determined in the presence of acetylcholine (AChCl) substrate. The unique nature of this approach lies in the enzyme immobilization procedure in which AChE was attached to the SPE by in situ bulk polymerization of acrylamide to ensure efficient adherence within the membrane with minimal losses in enzyme activity. Responses were observed for the pesticides Monocrotophos, Malathion, Metasystox and Lannate over the concentration range 0-10 ppb (microg L(-1)).

High-sensitivity chromatographic detector incorporating three-dimensional charge coupled device fluorimetry.

This article describes a detector for liquid chromatography that provides three-dimensional, excitation-emission-intensity data of fluorescent compounds. The instrument achieves multi-wavelength excitation by employing a polychromator that disperses radiation along the vertical portion of a quartz capillary flow cell. The ensuing sample fluorescence is collected in the horizontal plane and dispersed using an emission polychromator to form a focused two-dimensional excitation-emission image at a charge coupled device (CCD) pixel array. Each vertical pixel equates to a narrowly defined excitation wavelength band, whilst horizontal pixels equate to corresponding emission wavelengths, with the intensity of light encroaching onto the CCD pixel elements providing the third-dimensional variable in the measurement. It is shown that the extreme sensitivity of CCD detection coupled to the dual polychromator arrangement makes possible the collection of fluorescence excitation-emission-intensity data of polycyclic aromatic hydrocarbons in a flow stream in less than 0.05 s with nanogram per millilitre limits of detection.

Screen-printed amperometric biosensors for the rapid measurement of L- and D-amino acids.

Screen-printed three-electrode amperometric sensors incorporating L- and/or D-amino acid oxidase for the general purpose measurement of L- or D-amino acids is described. The working electrode incorporates rhodinized carbon, to facilitate hydrogen peroxide oxidation at a decreased operating potential, and immobilized enzyme. The devices responded to all 20 common L-amino acids and all of the D-amino acids examined, the exceptions being L- and D-proline. Linear response profiles were observed for L-leucine, L-glycine and L-phenylalanine with limits of detection of 0.47, 0.15 and 0.20 mM respectively. The devices were reproducible and exhibited stability over a 56 d test period. The biosensor compares favourably with a standard photometric amino acid test and was used to monitor milk ageing effects. The assay is cheap, simple to perform and rapid, requiring only buffer-electrolyte and a small sample volume.

Immunosensor for 2,4-dichlorophenoxyacetic acid in aqueous/organic solvent soil extracts.

The development of a simple electrochemical immunoassay procedure for the field-based quantification of the herbicide 2,4-D in methanolic soil extracts is presented. The sensor utilizes a competitive immunoassay format incorporating an immobilized antigen complex at the surface of a disposable screen-printed working electrode element. The extent of glucose oxidase-labeled antibody binding to the antigen--electrode is determined amperometrically and is related to sample analyte concentration. The performance of the sensor is assessed in buffer, 30% methanol, and methanolic soil extracts. The device is capable of quantifying 2,4-D in all three matrixes at the low ppm level with coefficient of variation values of 6.2-33.6%. The causes of the variation observed in the sensor response in different soil matrixes are examined and improvements proposed. The sensor, tested in parallel with a commercial 2,4-D immunoassay test kit, yields comparable quantitative data and detection limits while exhibiting greater assay simplicity.