Structural changes of soy proteins at the oil–water interface studied by fluorescence spectroscopy

Soy glycinin as food-grade Pickering stabilizers: Part. I. Structural characteristics, emulsifying properties and adsorption/arrangement at interface

“…Thus, it can be reasonably suggested that all the SG nanoparticles with high surface charge might exhibit a similar adsorption behavior to modified silica particles (nondeformed and spherical), rather than deformable and uncharged microgels. This can be indirectly consolidated by the previous observations that heated soy proteins or SPI aggregates did not suffer distinct changes in structural characteristics or morphology when adsorbed at the oil-water interface (Keerati-u-rai, Miriani, Iametti, Bonomi, & Corredig, 2012;Paunov et al, 2007). However, we can still see that the heat pretreatment at 100 C significantly decreased the %SC from 41.7% (unheated SG) to 32.5%, though there was no significant difference in % SC between the heated SG preparations at 90 and 100 C (Table 2).…”

Changes in the structure and dissociation of soybean protein isolate induced by ultrasound-assisted acid pretreatment

“…The emission fluorescence spectrum is mainly attributed to the tryptophan (Trp)/tyrosine (Tyr) residues and provides sensitive detection of protein conformational changes during processing (Keerati-u-rai, Miriani, Iametti, Bonomi, & Corredig, 2012). As shown in Fig.…”

Making sense of luminescence from GRAS optical probes

“…Shifts in the emission maxima of tryptophan fluorescence have been utilized to evaluate structural changes at the oil-water interface of soy-protein stabilized emulsions [38,39] before and after heat treatments. Fluorescent molecular rotors have been proposed to study stability of colloidal systems [23 ,40] and the fluorescence intensity of a presumptive GRAS molecular rotor, yellow #6 (sunset yellow FCF) was recently used to evaluate formation of surfactant assemblies [41].…”