Proteases, structure-function correlation

That is, we must learn how amino acid content and molecular configuration of food proteins are related to their functional properties. This goal is made more difficult by the fact that secondary, tertiary, and quarternary structures of proteins are likely to be quite different when exerting functional effects in food systems as compared to structures of the same proteins in dilute solutions and in their native states. The way in which specific actions of proteases affect protein structure must also be studied so that correlations with changes in functional properties can be made (61). 

The interaction between proteases and their inhibitors is, at least by comparison with interactions which take place in food systems, a remarkably simple and straightforward association. Simple correlations of functional properties with different kinds of molecular forces cannot be made. It is possible, however, to illustrate the importance of protein structure and of protein—protein interactions as determinants of the functional properties of food proteins. I would like therefore to look at several food systems in which protein—protein or protein—other constituent interactions play a role and examine the relationship between functionality and protein structure in these systems. One of the simplest areas in which to examine this relationship is the well studied collagen-gelatin transition. 

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