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Abstract
The main targets for the pressure induced changes in proteins are those regions primarily stabilised by hydrophobic and electrostatic interactions, since hydrogen bonds are almost pressure insensitive. Thus pressure treated proteins may well have very different structures to their native or heat treated counterparts and as a consequence different functionalities. This concept is used to discuss how pressure can modify the foaming, emulsifying and gelling properties of some food proteins and can also be used to modify the activity of some enzymes of importance in dictating food quality.