Quantification of protein-protein interactions in highly denatured whey and potato protein gels

Understanding the stabilizing protein interactions in protein gels is of high importance for food- and biotechnology. Protein interactions in protein gels can help to predict hardness, deformability and other gel parameters. Currently there are two types methods used. One is to use protein interaction blocking agents and the other is to dissolve the gel in different buffer systems, which cleave the interactions. The first method alters the gelling mechanism, which is why the second method is the preferred one. However, currently published methods are often only suitable for specific gel systems as for example weakly bound protein gels. In this paper, a method is introduced, which is suitable for highly denatured whey and plant protein.