Heat denaturation of soy glycinin: Influence of pH and ionic strength on molecular structure

The 7S/11S glycinin equilibrium as found in Lakemond et al. (J. Agric. Food Chem. 2000, 48, xxxx-xxxx) at ambient temperatures influences heat denatur ation. It is found that the 7S form of glycinin denatures at a lower temper ature than the 11S form, as demonstrated by a combination of calorimetric ( DSC) and circular dichroism (CD) experiments. At pH 7.6, at which glycinin is mainly present in the 11S form, the disulfide bridge linking the acidic and the basic polypeptides is broken during heat denaturation. At pH 3.8, a t which glycinin has dissociated partly into the 7S form, and at pH 5.2 thi s disruption does not take place, as demonstrated by solubility and gel ele ctrophoretic experiments. A larger exposure of the acidic polypeptides (Lak emond et al., 2000) possibly correlates with a higher endothermic transitio n temperature and with the appearance of an exothermic transition as observ ed with DSC. Denaturation/aggregation (studied by DSC) and changes in secon dary structure (studied by far-UV CD) take place simultaneously. Generally, changes in tertiary structure (studied by near-UV CD) occur at lower tempe ratures than changes in secondary structure.