Comparison of fibril aggregates from different soy materials

The aggregates of four kinds of soy protein from different production processes were formed with the different morphologies at low pH and heating at 90℃ for 10h. Thioflavin T (Th T) fluorescence, differential scanning calorimeter (DSC) , and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) were used to monitor the kinetics of aggregation and the protein compositions. The results indicated that protein compositions were remarkably different due to the different production processes. The glycinin (11S) , especially basic subunits inhibited the formation of fibril aggregates under the test condition. In addition, ionic strength played an important role in the formation of fibril aggregates.