Abstract:

Our previous study found that pectin with different degrees of esterification (DE) could affect the thermal aggregation of gluten, but the mechanism was not clear. Analyzing the thermal aggregation of glutenin and gliadin supplemented with pectin can clarify this mechanism. With the increase of temperature, the particle size, disulfide bonds and β-sheet of glutenins increased, the surface hydrophobicity (H0) and fluorescence intensity decreased, and the network gradually aggregated, but the change trend of gliadins was opposite. These results suggested that the thermal aggregation of gluten mainly depended on glutenin. Glutenin and gliadin supplemented with low ester pectin (LEP) were in an aggregated state. At 95 °C, LEP (DE = 37 %) increased the particle size of glutenin and gliadin (141.83 μm and 19.91 μm), promoted the conversion of thiol to disulfide bonds, increased β-sheet (34.01 % and 31.13 %), decreased fluorescence intensity (2186.33 and 5165.33) and H0 (49.65 and 369.26). Scanning electron microscope (SEM) indicated that glutenin and gliadin supplemented with LEP retained a dense network structure, especially glutenin. This study elucidated the specific mechanism of how pectin affected the thermal aggregation of gluten. These results provide a more comprehensive theoretical support and scientific basis for understanding how pectin regulates the final quality of gluten-based products.