Emulsifying Properties of Self-assembled Fibrillar Aggregates of Soy β-Conglycinin
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Abstract:
Soy β-conglycinin (7S) can self-assemble into amyloid-like fibrils with heat treatment, at a pH distant from the isoelectric point. The aim of this study was to investigate the potential application of 7S self-assembled fibrils in oil-in-water emulsions. 7S was heated at 85 ℃ for three hours (pH 2.0). The product was analyzed by dynamic light scattering (DLS), thioflavin T (Th T) fluorescence assay, and atomic force microscopy (AFM). The results indicated that short, rod-shaped, self-assembled fibrils were successfully prepared. The influence of protein concentration (c) and oil fraction (?) on the emulsifying activity and storage stability were studied using unheated 7S as well as 7S fibrils obtained from heat treatment as stabilizers. The results showed that at c ≥ 2%, the emulsifying activity of 7S-fibril was significantly higher than that of unheated 7S, which is probably since the linear fibrillar structure exhibits higher conformational flexibility and 7S-fibril can be effectively adsorbed onto the oil-water interface. At c = 6%, the droplet size (d4,3) was not affected by the ? value within the range of 0.2 to 0.6. At c ≥ 4.0%, 7S-fibril showed much higher emulsifying stability than unheated 7S along with relatively low coalescence index (CI) and creaming index (CI%) as compared to unheated 7S. Thus, 7S-fibril exhibited the properties of Pickering stabilizer. The results of this study indicate a new approach for the preparation of Pickering-like stabilizer.
