Wenjie He

The myofibrillar protein (MP) of duck meat is prone to excessive oxidation during thermal processing, resulting in a decline in its overall quality. In this paper, the effect of shikimic acid on the oxidative structure of duck muscle fibrin was studied. The findings showed that, at a mass ratio of 1:50,000 (g/g) between shikimic acid and MP, the carbonyl content of MP was reduced by 74.20%, while the sulfhydryl content was increased by 73.56%. MP demonstrated the highest denaturation temperature, whereas its thermal absorption was the lowest. The percentage of α-helixes and β-sheets increased by 16.72% and 24.74%, respectively, while the percentage of irregular structures decreased by 56.23%. In addition, the surface hydrophobicity index of MP exhibited a significant decrease (p < 0.05), while there was a significant increase in its free radical-scavenging ability (p < 0.05). Molecular fluorescence spectrum analysis showed that shikimic acid could bind to MP, altering the internal environment of MP and enhancing its thermal stability. FTIR analysis showed that shikimic acid could enhance the distribution of protein particle sizes by reducing irregular structures, the proportion of β-rotation, and the degree of protein aggregation. It is hoped that this research can offer scientific support for improving meat processing technology.

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.