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DENATURATION OF PLANT PROTEINS RELATED TO FUNCTIONALITY AND FOOD APPLICATIONS. A Review
Author(s) -
WU Y. VICTOR,
INGLETT GEORGE E.
Publication year - 1974
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1974.tb02861.x
Subject(s) - denaturation (fissile materials) , guanidine , chemistry , solubility , urea , optical rotation , covalent bond , protein tertiary structure , hydrochloride , soy protein , chromatography , organic chemistry , biochemistry , nuclear chemistry
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.