A recently-described immunoenzymatic (ELISA) method for the quantitative determination of biologically-active wheat germ agglutinin (WGA) in unknown samples has been applied to measure the concentration of active WGA in raw and cooked wheat-derived foodstuffs. The method exploits the binding specificity of WGA to ovalbumin as a first step followed by identification of bound lectin with polyclonal antibodies. Purified WGA was used to obtain calibration curves. Detectable amounts of WGA were found in raw foodstuffs and wheat flours, whilst variable amounts of agglutinin were found in wholemeal pasta probably as a consequence of thermal inactivation during food processing. The thermal gradient gel electrophoresis (TGGE) technique was therefore applied to analyse the thermal stability of WGA. The biological activity of WGA decreased as a function of heating temperatures and time of exposure to thermal treatment in an S-shaped fashion with an inflection point around 65 °C. As a consequence, WGA might represent a biochemical “indicator” allowing one to determine the thermal treatment undergone by wheat-derived foods during processing.
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