Formation, structure and functional characteristics of amyloid fibrils formed based on soy protein isolates.

ABSTRACT

Food protein-derived amyloid fibrils possess great untapped potential applications in food and other biomaterials. The objective of this report was to investigate the formation mechanism, structure and functional characterization of soy protein amyloid fibrils (SPF) through hydrolysis and heating (pH 2.0, 85 °C, 0-24 h) of soy protein isolate (SPI). Fibrillation growth analysis indicated polypeptide hydrolysis upon hydrolytic heating, and the amyloid fibrils were basically formed 8 h later. The microstructure of SPF was monitored by transmission electron microscopy and scanning electron microscopy, exhibiting change from an irregular spherical structure to a coiled, intertwined thread-like polymer. The secondary structures of SPI all changed drastically during the fibrillation process was characterized by Fourier transform infrared spectroscopy, which the α-helical and ß-turned content decreasing by 12.67 % and 5.07 %, respectively, and the content of ordered ß-folded structures increasing with heating time, finally increasing to 53.61 % at 24 h. The fluorescence intensity of the endogenous fluorescence spectra decreased and the maximum emission wavelength was red-shifted, suggesting that the fibrillation unfolded the protein structure, hydrolyzed and self-assembled into amyloid fibrils aggregates obscuring the aromatic amino acid residues. The emulsification activity, emulsion stability and viscosity of SPF improved with the increase in protein fibrillation.