Effects of pressure on protein structure

The main targets for the pressure induced changes in proteins are those reg ions primarily stabilised by hydrophobic and electrostatic interactions, si nce hydrogen bonds are almost pressure insensitive. Thus pressure treated p roteins may well have very different structures to their native or heat tre ated counterparts and as a consequence different functionalities. This conc ept 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 th e activity of some enzymes of importance in dictating food quality.