Methods to monitor process-induced changes in food proteins. An overview.
Proteins in food systems may undergo various changes in their structural properties as a consequence of processing. Whether these changes are beneficial or detrimental in terms of the nutritional, biological or functional properties of the processed system, it is important to apply analytical methods which can monitor the course of protein structural changes, in order to elucidate the underlying mechanism behind the results of different processes. Proteins are usually found in high concentrations in foods; furthermore, these proteins frequently may either initially be part of a solid food or may become insoluble due to processing. As a result, many of the traditional biochemical methods for analysis of protein structural properties in dilute solution cannot be applied directly to study food proteins. This chapter gives an overview of some potential methods which may be used to monitor the changes in quaternary, tertiary, secondary and primary structure of proteins in food systems.
Li-Chan
E C
EC
Department of Food Science, University of British Columbia, Vancouver, Canada.
D002942:Circular Dichroism; D004044:Dietary Proteins / Q000032:analysis*; D005504:Food Analysis / Q000379:methods*; D005511:Food Handling; D008027:Light; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013059:Spectrum Analysis, Raman; D014461:Ultracentrifugation
D004044:Dietary Proteins