Endogenous reactive oxygen species (ROS)-driven protein oxidation regulates emulsifying and foaming properties of liquid egg white.

Highly oxidative reactive oxygen species (ROS) attack protein structure and regulate its functional properties. The molecular structures and functional characteristics of egg white (EW) protein (EWP) during 28 d of aerobic or anaerobic storage were explored to investigate the "self-driven" oxidation mechanism of liquid EW mediated by endogenous ROS signaling. Results revealed a significant increase in turbidity during the storage process, accompanied by protein crosslinking aggregation. The ROS yield initially increased and then decreased, leading to a substantial increase in carbonyl groups and tyrosine content. The free sulfhydryl groups and molecular flexibility in EWP exhibited synchronicity with ROS production, reflecting the self-repairing ability of cysteine residues in EWP. Fourier-transform infrared spectroscopy indicated stable crosslinking between EWP molecules in the early oxidation stage. However, continuous ROS attacks accelerated EWP degradation. Compared with the control group, the aerobic-stimulated EWP showed a significant decrease in foaming capacity from 30.5 % to 9.6 %, whereas the anaerobic-stimulated EWP maintained normal levels. The emulsification performance exhibited an increasing-then-decreasing trend. In conclusion, ROS acted as the predominant factor causing deterioration of liquid EW, triggering moderate oxidation that enhanced the superior foaming and emulsifying properties of EWP, and excessive oxidation diminished the functional characteristics by affecting the molecular structure.

Polysaccharide-addition order regulates sonicated egg white peptide stabilized nanoemulsions and ß-carotene digestion in vitro.

In this paper, the effects of the polysaccharide-addition order (before and after homogenisation) on the stability of nanoemulsion stabilised by sonicated egg white peptides and the in vitro digestive behaviour of loaded ß-carotene were investigated. The pyrene fluorescence results showed that the concentration of micelles formed by flaxseed gum (FG) in complex with peptides was significantly higher than that of peach gum (PG). The order of polysaccharide-addition affected the emulsion properties and stability; adding polysaccharides before homogenisation led to protein bridging flocculation, low polysaccharide coverage and a higher interfacial adsorbed protein content of the emulsion. PG enhanced potential spatial resistance and electrostatic repulsion, effectively prevented emulsion flocculation and improved electrostatic stability. After homogenisation, FG was added to emulsions to improve environmental stability, including ionic, temperature and storage stability. Due to the viscosity of polysaccharides and the formed polysaccharide-protein-lipid aggregates, the increasing degree of bridging flocculation promoted the prominent of apparent viscosity, and the G' and G'' exhibited a frequency-dependent increase. The polysaccharide type and mode changed the surface loading charge and droplet interface thickness, delayed the destruction of the droplet structure by protease, and slowed the release of ß-carotene to form micelles. In this study, a stable emulsion system and an efficient emulsion transport system for bioactive substances were obtained by regulating polysaccharides adding order, which is significant for constructing an efficient food emulsion delivery system.

The relationship between acylation degree and gelling property of NaOH-induced egg white gel: Efficient is better?

In this study, succinic anhydride (SA) and octenyl succinic anhydride (OSA) were used to modify the egg white protein (EWP), and acylated EWP was further prepared as a gel by adding NaOH and heat modification. The results showed that the acylation degree for the SA- and OSA-added groups reached 57.68% and 26.95%, respectively, and the average size, the absolute value of ζ-potential, increased significantly with SA and OSA addition, indicating that acylation improved the stability of EWP solution. Furthermore, the surface hydrophobicity increased for the SA-added group while decreasing for the OSA-added group, and the acylation process exposed the flexibility part of the protein molecule. Acylated EWP prepared gel (EWG) showed a translucent and slightly yellow appearance (except for the sol state of the OSA-added 1:50 group), the gel strength, water-holding capacity and rheological properties for SA-added EWG were remarkably reduced while OSA-added EWG improved apparently. Intermolecular forces analysis indicated that the addition of SA promoted the formation of disulfide bonds and strengthened proteins interactions while adding OSA weakened the interactions. Microstructural observations revealed a rougher gel network structure and weaker protein cross-linking in the gel prepared after the acylation of proteins. However, the high efficiency of SA and promotion of protein-molecule interactions were unable to counteract the negative effect of SA on the extension of the gel network structure, and the interaction between OSA expanded the formation of the gel network structure.

Phosphorylation modification affects the gelation behavior of alkali-induced duck egg white gels.

In this study, sodium tripolyphosphate (STP) and tetrasodium pyrophosphate (TSPP) were utilized to modify duck egg white protein (EWP). The phosphorylated EWP was prepared as egg white gel (EWG) by adding sodium hydroxide. The phosphorus content of EWP reached 2.18 mg/g and 2.07 mg/g with the addition of STP and TSPP, respectively, after 2 h phosphorylation. The average particle size, absolute zeta potential value, and surface hydrophobicity of EWP increased significantly during phosphorylation. FTIR results indicate that phosphorylation reduced the random structure and α-helical content while increasing the content of ß-sheets and ß-turn. The mechanical and rheological properties of EWG decreased obviously after phosphorylation. A three-dimensional porous network microstructure was formed, and the gel with added TSPP had larger pores. Adding STP and TSPP to EWG weakened its salt and solvent sensitivity. The findings provide a direction for the exploration of gel properties after protein modification.

Characteristics of intermolecular forces, physicochemical, textural and microstructural properties of preserved egg white with Ca(OH)2 addition.

The effects of Ca(OH)2 on the physicochemical, mechanical and microstructural characteristics, intermolecular forces and protein patterns of preserved egg white (PEW) were investigated. Results suggested that Ca(OH)2 (0.1%) reduced the free alkalinity content and turbidity and increased the brightness of PEW. The surface hydrophobicity of PEW protein with added Ca(OH)2 decreased during the pickling period owing to the hydrophobic residues being hidden in the interior of the protein. Total content of sulfhydryl and disulfide bonds in PEW decreased. Non-specific cross-linking, hydrogen bonds and hydrophobic interactions were the primary intermolecular forces. For textural properties, hardness and springiness had obvious prominence. A loose porous and regular network-like microstructure formed as the Ca(OH)2 increased and Ca(OH)2 delayed denaturation of the PEW protein. The physical properties of PEW correlated with molecular interactions and the microenvironment. Ca(OH)2 improved the contribution of surface hydrophobicity, disulfide bonds and hydrophobic interactions to the gelation process.