In this study, disulfide bonds between the interfacial protein film formed on the lipid particles and the protein in ovalbumin emulsion gels were blocked with 0, 1, 3, 5 and 10 mM of the N -ethylmaleimide (NEM) to explore the influence and effect mechanism of disulfide bonds between the interfacial proteins on the physicochemical properties, microstructure, and protein structure of sunflower oil–ovalbumin emulsion gels. Ovalbumin emulsion gels with NEM-treated ovalbumin emulsion (N-OE) had lower hardness, free sulfhydryl content, water holding capacity (WHC), and surface hydrophobicity , but higher spin−spin relaxation time ( T 2 ) than ovalbumin emulsion gels with NEM-treated ovalbumin substrate solution (N-OSS). In addition, N-OE and N-OSS had lower hardness, free sulfhydryl content, WHC and surface hydrophobicity, as well as a more coarse and disordered microstructure than non-NEM treated ovalbumin emulsion gel (control group). The free sulfhydryl content, hardness, WHC, and surface hydrophobicity of the ovalbumin emulsion gels all decreased as the NEM concentration rose ( p < 0.05), whereas the amide A band changed to higher wave numbers. These results collectively indicated that the reduction of disulfide between the interfacial layer and the proteins inhibited the hydrophobic effect , the formation of hydrogen bonds , and prevented the formation of larger aggregates. Thus the disulfide bonds between the interfacial proteins contribute to the hardness enhancement and water stabilization of the ovalbumin gel.
To investigate the effect of oil droplets surface film type and droplets size on the physicochemical properties and digestibility of thermally induced ovalbumin–oil emulsion gels, Tween 80 and ovalbumin were selected as individual emulsifiers for the emulsification of sunflower oil at different homogenization speeds (6000, 8000, and 10000 rpm), and the formed emulsions were mixed with ovalbumin matrix solution and then heated to form heat-induced ovalbumin emulsion gels (OEG). The OEG with ovalbumin as emulsifier had higher hardness, water holding capacity (WHC), and surface hydrophobicity, and lower digestibility, spin−spin relaxation time ( T 2 ) and free sulfhydryl content than those of the OEG with Tween 80 as the emulsifier ( p < 0.05). As the oil droplets size decreased, the hardness increased, WHC increased, the amide A band shifted to lower wavenumbers, digestibility decreased, T 2 decreased, free sulfhydryl content decreased, and surface hydrophobicity increased for both OEG ( p < 0.05). These results collectively indicated that the physicochemical properties of the OEG are influenced by the property of the oil interfacial film and the size of the oil droplets. The oil droplets surrounded by the interfacial protein film improved the performance of the OEG greatly, and the proteins within its OEG formed a dense gel network structure through hydrophobic aggregation, disulfide bond crosslinking, and hydrogen bonding. The oil droplets with smaller sizes favored the enhancement in the physicochemical properties of the OEG. Changes in the size of oil droplets and the type of film wrapped around them regulated the digestibility of the OEG.
危险品化学品经营许可证（带存储）