The self-assembly fibrillar aggregations of soy glycinin and β-conglycinin at pH 2.0,85 ℃ with various protein concentrations were investigated using dynamic light scattering(DLS) and Thioflavin T fluorescence techniques.The heat-induced gelation properties including rheology,hardness and network structure of different fibrillar aggregations were characterized simultaneously.The results showed that protein concentration played an important role in the self-assembly aggregate formation at low pH and low ionic strength.The data suggested fibrillar aggregation progressively increased with the increasing of protein concentration.β-Conglycinin exhibited a higher ability to form thermally fibrillar aggregates than glycinin.The increasing degree of fibrillar aggregate was favorable for enhancing the network structure of heat-set gels.The hardness of glycinin fibril gel was stronger than that of β-conglycinin.Scanning electron microscopy observation indicated that the network of β-conglycinin fibril gel was more compact than glycinin,while the latter one was more in order.