Role of the Thermal Denaturation‐Aggregation Relationship in Determining the Rheological Properties of Heat Induced Networks for Ovalbumin and Vicilin

Heat‐induced denaturation (determined by differential scanning calorimetry plus ANS fluorescence) and structure development (assessed by dynamic testing) were monitored for ovalbumin and vicilin to evaluate the importance of these processes on the rheological characteristics of resulting protein networks. Protein denaturation preceded structure development, based on an increase in the storage modulus (G′). Reduction of the temperature between denaturation and aggregation through pH manipulation or inclusion of stabilizing salts lowered G′ values in the resulting network. In contrast, in the presence of SDS, G′ values increased with (ovalbumin) or were unrelated to (vicilin) reduced temperature differences. This demonstrated the importance of a balance of attractive and repulsive forces when examining network characteristics.