DENATURATION OF PLANT PROTEINS RELATED TO FUNCTIONALITY AND FOOD APPLICATIONS. A Review

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Abstract
Proteins can be denatured by heat, changes in pH, organic solvents, detergents, urea, guanidine hydrochloride or other methods that modify the secondary, tertiary or quaternary structure, without breaking any covalent bonds. Physical‐chemical measurements or functionality related to denaturation include solubility, viscosity, dissociation into subunits, sedimentation constant, optical rotation, association and ultraviolet spectra. The relationship between pH, temperature and rate of denaturation of wheat and soy proteins is complex. Optimum heat treatment of soy flakes, for example, inactivates nearly all biologically active components, but the protein retains most of its functionality. Knowledge about protein denaturation helps to produce food products with desirable functional properties.