This article reviews recent developments in the application of capillary electrophoresis (CE) for the analysis of foods and food components. CE has been applied to a number of important areas of food analysis and is fast becoming an established technique within food analytical and research laboratories. Papers are reviewed that were published during the two years to date following the previous review (Electrophoresis 2001, 22, 4197-4206).

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Surface plasmon resonance (SPR) plays a dominant role in real-time interaction sensing of biomolecular binding events. This book focuses on a total system description including optics, fluidics and sensor surfaces. It covers all commercial SPR systems in the market. It is the first of its kind and fills a gap in the technical literature as no other handbook on SPR is currently available. The final chapter discussed new trends and a vision is given for future developments and needs of the SPR market. This excellent handbook provides comprehensive information with easy to use, stand-alone chapters and will be of great use to anyone one working with or affiliated to the technology.

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This review article addresses recent advances in the analysis of foods and food components by capillary electrophoresis (CE). CE has found application to a number of important areas of food analysis, including quantitative chemical analysis of food additives, biochemical analysis of protein composition, and others. The speed, resolution and simplicity of CE, combined with low operating costs, make the technique an attractive option for the development of improved methods of food analysis for the new millennium.

Surface plasmon resonance (SPR) has been employed to investigate the hydrolytic degradation of thiolated dextran monolayers on silver by the enzyme dextranase. The influence of pH upon the kinetics of this enzyme-catalyzed degradative reaction has been demonstrated, and SPR experiments reveal that dextranase does not completely remove the thiolated dextran monolayers, even at the enzyme's most active pH. X-ray photoelectron spectroscopy and atomic force microscopy results support this observation, as do SPR measurements of protein adsorption to degraded samples, which show significant protein resistance after degradation. It is suggested that incomplete degradation occurs due to an inability of the enzyme to process, or complex with, the derivatized thiol bound portions of individual dextran macromolecules close to the silver surface.

Atomic force microscopy has been employed for the in situ investigation of the molecular hydration of thiolated dextran monolayers within a liquid environment. The studies have demonstrated the ability to measure corresponding changes in both monolayer morphology and elasticity due to the hydration state of dextran. Imaging in water allows the visualization of macromolecular swelling, matched by an increase in surface elasticity monitored via the analysis of force-distance curves. Subsequent imaging in a propanol environment leads to dehydration effects observed through a relaxation of swelling and a decrease in surface elasticity.

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