Egg-white protein has an abundance of hydrophobic amino acids and could be a potential emulsifier after modification. Here, egg-white protein was modified via ultrasonic and transglutaminase treatments to destroy the globular structure. The egg-white protein gel particles (EWP-GPs) were prepared and then a novel highly stable EWP-chitosan double-layer emulsion was constructed. When ultrasonic treatment was applied at 240 W and TGase (20 U/g EWP) treatment, the EWP-GPs had a low particle size and good emulsification performance. The particle size of EWP-GPs was a minimum of 287 nm, and the polymer dispersity index (PDI) was 0.41. The three-phase contact angle (θ_o/w) of EWP-GPs was 79.6° (lower than 90°), performing with good wettability. Based on these results, the EWP-chitosan double-layer emulsion was prepared through the EWP-GPs being treated with 240 W ultrasound, TGase, and chitosan in this study. When the double-layer emulsion had 0.6% (v/v) chitosan, the zeta potential of the double-layer emulsion was −1.1 mV and the double-layer emulsion had a small particle size (56.87 µm). The creaming index of double-layer emulsion at 0.6% (v/v) chitosan was 16.3% and the droplets were dispersed uniformly. According to the rheological results, the storage modulus (G′) was larger than the loss modulus (G″) in the whole frequency, indicating the formation of an elastic gel network structure in the emulsion. It is hoped to develop a novel food-grade stabilizer and a stable double-layer emulsion, providing new environment-friendly processing in hen egg products and delivery systems.

The effect of fenugreek (Trigonella foenum-graecum L.) seed extracts (FSEs) on the structure of duck myofibrillar protein (MP) oxidation was researched via particle size, zeta potential, Fourier transform infrared (FTIR), fluorescence spectroscopy, SDS-PAGE, and scanning electron microscopy (SEM) in the Fenton oxidation system. FSE (0.3 mg/mL) could scavenge 58.79% of the hydroxyl radical and possessed good antioxidation. FSE could retard the oxidation of MP, and the carbonyl formation and total sulfhydryl loss of MP decreased by 42.00% and 105.94%, respectively, after 4.67% of FSE treatment. SDS-PAGE results showed that 0.67% and 2.67% of FSE decreased the strength of the myosin heavy chain (MHC) and actin bands of the oxidized MP, respectively. The FSE changed the secondary structures of the MP and promoted the unfolding of the MP structure and the transformation from α-helix to β-turn. When treated with 0.67% of FSE, the hydrophobicity of the MP declined by 26.14%, and solubility was improved by 37.21% compared with the oxidation group. After 0.67% of FSE treatment, the particle size and zeta potential of the MP returned to the level of the blank group. Scanning electron microscopy revealed that FSE improved the apparent morphology of the MP. Overall, FSE had positive effects on the antioxidation of the duck MP, and it could improve the structure and characteristics of the MP. It is hoped that FSE could be considered as a natural antioxidant to retard the oxidation of the MP in meat products.

Spice and its extracts have gained widespread utilization as natural and eco-friendly additives, imparting enhancements in flavor, color, and antioxidative attributes to meat-based products. This work aims to study the effect mechanism of capsaicin (CA) and dihydrocapsaicin (DI) in capsicum (chili pepper) on the structure and function of myofibrillar proteins (MPs) in duck meat during thermal treatment. The results showed that at a CA–DI to MP ratio of 1:500 (g/g) following a 12 min heat treatment, the carbonyl content of MPs in duck meat decreased by 48.30%, and the sulfhydryl content increased by 53.42%. When the concentration was 1:500 (CA-DI, g/g) after 24 min of heat treatment, the •OH and DPPH radical scavenging rates were highest at 59.5% and 94.0%, respectively. And the initial denaturation temperature of MPs was the highest at 96.62 °C, and the thermal absorption was lowest at 200.24 J g⁻¹. At the parameter, the smallest particle size and size distribution range of MP were 190 nm (9.51%). Furthermore, the interplay between CA–DI and MPs contributed to a reduction in the protein particle size and intrinsic fluorescence. In summary, the combination of CA–DI and MPs played a crucial role in inducing protein unfolding and disintegration.