Liping Luo

Effectiveness of partially hydrolyzed rice glutelin as a food emulsifier: Comparison to whey protein

The emulsifying properties of partially hydrolyzed rice glutelin (H-RG, 2% degree of hydrolysis) were compared to those of whey isolate protein (WPI), a commonly used protein-based emulsifier. The surface load of WPI (1% emulsifier, d32=167.5nm) was 2.8 times lower than that of H-RG (3% emulsifier, d32=159.0nm). Emulsions containing WPI-coated lipid droplets had better stability to pH changes (2-8), NaCl addition (0-500mM) and thermal processing (30-90°C, 0 or 200mM NaCl). Nevertheless, H-RG emulsions were stable over a range of conditions: pH 6-8; NaCl≤200 (pH 7); temperatures≤90°C in the absence of salt (pH 7); and temperatures≤50°C in the presence of 200mM NaCl (pH 7). This study indicates that H-RG may be utilized as a natural emulsifier in the development of label-friendly emulsion-based food products, but that further work is needed to increase the range of applications.

Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes

The interaction of rice glutelin (RG) with amylose was characterized by spectroscopic and molecular docking studies. The intrinsic fluorescence of RG increased upon the addition of amylose. The binding sites, binding constant and thermodynamic features indicated that binding process was spontaneous and the main driving force of the interaction was hydrophobic interaction. The surface hydrophobicity of RG decreased with increasing amount of amylose. Furthermore, synchronous fluorescence and circular dichroism (CD) spectra provided data concerning conformational and micro-environmental changes of RG. With the concentration of amylose increasing, the polarity around the tyrosine residues increased while the hydrophobicity decreased. Alteration of protein conformation was observed with increasing of α-helix and reducing of β-sheet. Finally, a visual representation of two binding sites located in the amorphous area of RG was presented by molecular modeling studies.