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denatures the protein (structurally) becomes inactive
A protein manifests functionality by interacting with other compnents within the food system. These interactions may involve solvent molecules, solute molecules, other protein molecules or substances that are dispersed in the solvent such as oil or air.In order to describe the forces involved in these interactions, it is essential that the forces and energies involved in the achievement and maintenance of native protein structure be described. While a complete discussion of the forces involved is beyond the scope of this chapter, some observations on the nature of protein structure will be useful.Proteins exist in the lowest kinetically attainable state of free energy. The free energy of the protein may not be the global minimum, but it will be the lowest that the protein can achieve in a reasonable period of time.Protein structure is highly dependent upon the environment and the protein will assume different conformation as the environmental conditions change. Factors of importance include pH, temperature, dielectric constant, ionic strength and the presence of other molecules including air, fat, denaturants, etc. One of the main ways that proteins lower their free energy involves the removal the removal of hydrophobic groups from the aqueous environment. This may provide the greatest single decrease in free energy of all the types of binding that occur within proteins. The strength of hydrophobic binding is, however, very sensitive to changes in temperature and dielectric constant and thus changes in these parameters can have large influences on protein structure.
Woah too much information my brain hurts O.o