Fibrillar Aggregation Behavior and Stability of Soy Globulin
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Abstract:
In order to better define fibrillar aggregation behavior of protein, the heat-induced soy globulin (11S) fiber aggregation process under acidic conditions was investigated in the subunit level to monitor the hydrolysis process, structural change and stability of the protein and its subunits by using 11S as raw material. The hydrolysis kinetics results showed that the fibrillar aggregation process of 11S was a multistep process, including the hydrolysis of polypeptide chains, self-assembly into amyloid fibrils aggregates and the gradual accumulation of macroscopically visible fibrous aggregates with twisted helical structures. Compared with the single exponential growth of the 11S fibrosis process, the fibrosis process of the acidic subunits was delayed. The acidic subunits mainly contributed to the nucleation process of fibril aggregation in the early stage, while the addition of basic subunits could change the process of fibril aggregation. The fibril aggregates of protein could increase the solubility of 11S at isoelectric point and decrease the solubility at neutral acidic pH. In addition, the alkaline environment (pH 10.0) would cause 11S fiber aggregates to dissolve completely, and the macroscopic fiber length becomes shorter and the structure changes. The results might provide a theoretical basis for the rational use of soy protein fibril aggregates as a novel functional food ingredient.
