Substitution of sucrose by erythritol in angel cake: Effect on protein foaming, baking performance and digestion properties.

Sugars played an important role in the processing of products such as cakes, however, their high-calorie character often posed a health risk to consumers. Therefore, this paper aimed to better investigate the effect of sugar substitutes on the improvement of egg white foaming properties and angle cake digestibility characteristics. It was demonstrated that the addition of erythritol improved the surface properties of egg whites, thus enhancing their foaming properties. Particularly, when the erythritol substitution was 50 %, the sugar-egg white complex structure unfolded and had the best foaming capacity. On this basis, the baking performance of angel cakes with sucrose replaced by erythritol was analyzed. When the erythritol substitution was lower than 50 %, the specific volume and the baking loss rate of the cakes were basically unchanged, and the texture and sensory taste of the cakes were all excellent. Finally, the gastrointestinal digestive kinetic analysis suggested that erythritol substitution for sucrose was beneficial for reducing blood glucose levels in vivo. Furthermore, for the MgCl2-based samples, both the degree of protein destruction after digestion was weakened and the glucose-lowering effect was better exerted. Overall, this study provided a new theoretical basis for the low-calorie sugar-substituted health food products development in the future.

Magnesium ions regulated ovalbumin-lysozyme heteroprotein complex: Aggregation kinetics, thermodynamics and morphologic structure.

This study aims to investigate the mechanism of magnesium ions regulated ovalbumin-lysozyme (OVA-LYS) heteroprotein aggregation behavior via aggregation kinetics model, exploring the relationship between differential aggregation behavior and protein molecular structure, intermolecular interactions and thermal stability. Results showed that the aggregation rate (kapp) and maximum absorbance (Amax) of the OVA-LYS heteroprotein complex were located between OVA and LYS. Meanwhile, the thermal denaturation temperature (Td) and denaturation enthalpy (ΔH) were between the values of OVA and LYS as well. Compared with OVA, the thermal stability of the OVA-LYS heteroprotein complex increased owing to the electrostatic interactions between OVA and LYS, resulting in slower aggregation rate and lower aggregation degree. Molecular dynamics simulations revealed the molecular conformational changes during OVA-LYS binary protein binding and the stability of the complex conformation. Moreover, MgCl2 weakened the OVA-LYS interactions through Debye shielding while increasing thermal stability, allowing the two proteins to aggregate into amorphous precipitates rather than spherical coacervates. Overall, this study provides information to further understand the regulation mechanism of proteins differential aggregation behavior by ions.