In the development of new foods or in the control of traditional process, protein functionality plays a paramount role. It has long been theorized that changes in protein structure can alter functionality, but there has been a lack of reliable methodologies for observing protein structural changes in ‘real-world’ food samples. Here, a technique for determination of the global secondary structure of proteins using Fourier transform infrared (FTIR) spectroscopy in H2O instead of D2O is assessed and contrasted with other methodologies for structural determinations. A quantitative procedure is presented for preparing and analysing FTIR spectra of proteins for the determination of their global secondary structural components. As an example, an analysis of the FTIR spectra of egg-white lysozyme is presented and correlated with global secondary structure values calculated from its X-ray crystallographic structure. Other examples of FTIR analyses of food proteins are presented with consideration given to qualitative procedures for more rapid structural analysis of processed samples.
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