In this study, changes in hydrophobic interactions among gluten proteins were analyzed during dough mixing. Size-exclusion high-performance chromatography and two-dimensional fluorescence difference gel electrophoresis were performed on proteins extracted with 1-propanol by weakening the hydrophobic interaction. The amount of proteins extracted with 30% 1-propanol increased from the start of mixing to peak consistency, suggesting that the hydrophobic interactions among the strongly aggregated proteins weakened and resulted in disaggregation. The amount of proteins extracted with 10% 1-propanol decreased during hydration, indicating that these proteins aggregated through relatively weak hydrophobic interactions. The proteins that extractability decreased were mainly low molecular weight glutenin, α-gliadin, and γ-gliadin. The amount of monomeric proteins extracted with 30% 1-propanol decreased after peak consistency. The decreased protein was mainly ω-gliadin, indicating that ω-gliadin aggregated with other proteins through hydrophobic interactions. A front-face fluorescence analysis was performed on the dough with the addition of 8-anilino-1-naphthalenesulfonic acid or thioflavin T. The fluorescence intensity increased as a result of exposure to the hydrophobic groups of the gluten proteins and the formation of protein aggregates during dough mixing. These results indicate the importance of hydrophobic interactions in dough formation.

中文翻译：

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面团形成过程中面筋蛋白之间疏水相互作用的变化

在这项研究中，分析了面团混合过程中面筋蛋白之间疏水相互作用的变化。通过减弱疏水相互作用，对1-丙醇提取的蛋白质进行尺寸排阻高效色谱和二维荧光差异凝胶电泳。用 30% 1-丙醇提取的蛋白质的量从混合开始到峰值一致性增加，表明强聚集蛋白质之间的疏水相互作用减弱并导致解聚。在水合过程中，用 10% 1-丙醇提取的蛋白质数量减少，表明这些蛋白质通过相对较弱的疏水相互作用聚集。可提取性降低的蛋白质主要是低分子量麦谷蛋白、α-麦胶蛋白和γ-麦胶蛋白。峰一致性后，用 30% 1-丙醇提取的单体蛋白质的量减少。减少的蛋白质主要是ω-麦胶蛋白，表明ω-麦胶蛋白通过疏水相互作用与其他蛋白质聚集。对添加 8-anilino-1-naphthalenesulfonic acid 或 thioflavin T 的面团进行正面荧光分析。 由于暴露于面筋蛋白的疏水基团和蛋白质聚集体的形成，荧光强度增加在面团搅拌过程中。这些结果表明疏水相互作用在面团形成中的重要性。对添加 8-anilino-1-naphthalenesulfonic acid 或 thioflavin T 的面团进行正面荧光分析。 由于暴露于面筋蛋白的疏水基团和蛋白质聚集体的形成，荧光强度增加在面团搅拌过程中。这些结果表明疏水相互作用在面团形成中的重要性。对添加 8-anilino-1-naphthalenesulfonic acid 或 thioflavin T 的面团进行正面荧光分析。 由于暴露于面筋蛋白的疏水基团和蛋白质聚集体的形成，荧光强度增加在面团搅拌过程中。这些结果表明疏水相互作用在面团形成中的重要性。