Heat-Induced Fibrillar Aggregation of 7S Globulins (vicilins) from Phaseolus Legumes
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Abstract:
The heat-induced fibrillar aggregations of 7S Globulins (vicilins) from kidney bean (Gk) and mung bean (Gm) at low pH and low ionic strength were characterized using dynamic light scattering (DLS), Thioflavin T (Th T) fluorescence assay and atomic force microscopy (AFM). According to thermal characteristics and phase diagram analysis, 85 °C and 0.5% were chosen as denaturation temperature and proper protein concentration. Results also showed that heating led to fibrillar aggregation. Th T maximum fluorescence intensity of Gk and Gm increased dramatically to 765 and 1093 within one hour, indicating that the building blocks were formed at the initial heating periods. DLS data suggested Gk exhibited stronger ability of self assembly and fibrillar aggregation. However, the extent of aggregation and morphology of formed fibrils varied distinctly. AFM data displayed clearly that Gk formed linear fibrils but Gm formed random fibrils upon heating for 12h. This would give experiment data for preparation of transparent gels at extremely low weight fractions plant proteins based on self-assembly.
