Heating Rate Affects Thermal Properties and Network Formation for Vicilin and Ovalbumin at Various pH Values

The impact of heating rate on the strength and type of networks formed with ovalbumin and vicilin were investigated at three pH levels. Changes in protein conformation and structure development were monitored with differential scanning calorimetry (DSC) and dynamic rheology. Networks were characterized by rheological properties and microstructure. Under conditions which promoted the formation of well crosslinked networks, slower heating rates resulted in stronger networks but had little impact on the type of network. As conditions were shifted to promote aggregation rather than network formation, the impact of heating rate was reduced so that for both ovalbumin and vicilin at pH 5, network characteristics were essentially independent of heating rate.