Chen Jinfeng, Shi Wanlu, Shen Zheyu, Ma Yunxiang, Zhang Shenggui
College of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, Gansu, People's Republic of China; State Key Laboratory of Aridland Crop Science, Lanzhou 730070, Gansu, People's Republic of China.
College of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, Gansu, People's Republic of China.
Int J Biol Macromol. 2025 Jan;286:138394. doi: 10.1016/j.ijbiomac.2024.138394. Epub 2024 Dec 4.
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 (H) 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 H (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.
我们之前的研究发现，不同酯化度（DE）的果胶会影响面筋蛋白的热聚集，但机制尚不清楚。分析添加果胶的谷蛋白和醇溶蛋白的热聚集可以阐明这一机制。随着温度升高，谷蛋白的粒径、二硫键和β-折叠增加，表面疏水性（H）和荧光强度降低，网络逐渐聚集，而醇溶蛋白的变化趋势相反。这些结果表明，面筋蛋白的热聚集主要取决于谷蛋白。添加低酯果胶（LEP）的谷蛋白和醇溶蛋白处于聚集状态。在95℃时，LEP（DE = 37%）增加了谷蛋白和醇溶蛋白的粒径（分别为141.83μm和19.91μm），促进了硫醇向二硫键的转化，增加了β-折叠（分别为34.01%和31.13%），降低了荧光强度（分别为2186.33和5165.33）以及H（分别为49.65和369.26）。扫描电子显微镜（SEM）表明，添加LEP的谷蛋白和醇溶蛋白保留了致密的网络结构，尤其是谷蛋白。本研究阐明了果胶影响面筋蛋白热聚集的具体机制。这些结果为理解果胶如何调节面筋基产品的最终品质提供了更全面的理论支持和科学依据。
