This review examines the applications of electronic noses and tongues in food analysis. A brief history of the development of sensors is included and this is illustrated by descriptions of the different types of sensors utilized in these devices. As pattern recognition techniques are widely used to analyse the data obtained from these multisensor arrays, a discussion of principal components analysis and artificial neural networks is essential. An introduction to the integration of electronic tongues and noses is also incorporated and the strengths and weaknesses of both are described. Applications described include identification and classification of flavour and aroma and other measurements of quality using the electronic nose. The uses of the electronic tongue in model analyses and other food, beverage and water monitoring applications are discussed.

Pharmaceutical counterfeiting is becoming a serious problem both in developed and developing countries. This paper considers the extent of the problem and provides several examples of drugs which have been counterfeited. Additionally, the effects of counterfeit products on consumers, health care providers, drug manufacturers and governments are discussed. Several of the currently used methods of detection are described and these include near-infrared spectroscopy, Raman spectroscopy, isotopic characterization, tensiography, chromatographic and mass spectrometric approaches. Finally, anti-counterfeiting measures such as the use of holograms, tracers and taggants and electronic tracking are summarized.

In recent years, a number of new methods have been reported that make use of immobilized enzymes either on microarrays or in bioaffinity columns for high-throughput screening of compound libraries. A key question that arises in such methods is whether immobilization may alter the intrinsic catalytic and inhibition constants of the enzyme. Herein, we examine how immobilization within sol-gel-derived materials affects the catalytic constant (kcat), Michaelis constant (KM), and inhibition constant (KI) of the clinically relevant enzymes Factor Xa, dihydrofolate reductase, cyclooxygenase-2, and gamma-glutamyl transpeptidase. These enzymes were encapsulated into sol-gel-derived glasses produced from either tetraethyl orthosilicate (TEOS) or the newly developed silica precursor diglyceryl silane (DGS). It was found that the catalytic efficiency and long-term stability of all enzymes were improved upon entrapment into DGS-derived materials relative to entrapment in TEOS-based glasses, likely owing to the liberation of the biocompatible reagent glycerol from DGS. The KM values of enzymes entrapped in DGS-derived materials were typically higher than those in solution, whereas upon entrapment, kcat values were generally lowered by a factor of 1.5-7 relative to the value in solution, indicating that substrate turnover was limited by partitioning effects or diffusion through the silica matrix. Nonetheless, the apparent KI value for the entrapped enzyme was in most cases within error of the value in solution, and even in the worst case, the values differed by no more than a factor of 3. The implications of these findings for high-throughput screening are discussed.

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