河南工业大学粮油食品学院刘昆仑教授团队在Food Hydrocolloids发表题目为“Comparison of formation and structural characteristics of amyloid fibrils of peanut protein isolate after hydration treatment at different pH”研究论文（不同pH水化处理后花生分离蛋白淀粉样纤维的形成及结构特征比较）。摘要： 本文研究了pH 5.0（Q组）和pH 2.0（S组）水化处理后花生蛋白的原纤维化过程及所形成原纤维的结构，结果表明：与pH 5.0水化处理的花生蛋白相比，pH 2.0水化处理的花生蛋白粒径增大，表面疏水性和固有荧光强度降低，表明蛋白质发生了聚集。在纤维化过程中，Q组蛋白的Thioflavin T最大荧光强度高于S组，S组蛋白达到最大荧光强度的时间晚于Q组蛋白；且Q组蛋白先形成短的蠕虫状纤维后形成长的柔性纤维，S组蛋白先形成短的刚性纤维后形成蠕虫状纤维。综上所述，pH 2.0水化处理导致花生蛋白发生聚集，降低了花生蛋白的纤维形成能力，并影响了后续的自组装过程。本研究可为不同pH水化处理后花生蛋白纤维形成机理和结构特性提供新的见解。研究结果：3.1 ThT荧光测定Fig. 1. ThT fluorescence intensity of Q and S after thermal treatment at pH 2.0 and 85 °C for 0–12 h.3.2. SDS-PAGEFig. 2. SDS-PAGE gel (reducing) of Q and S after fully hydrated, centrifuged and filtered membrane.3.3 粒度分析Fig. 3. Particle size of Q and S after thermal treatment at pH 2.0 and 85 °C for 0–12 h.3.4. 二级结构Fig. 4. CD spectra and Secondary structure distributions of Q and S after thermal treatment at pH 2.0 and 85 °C for 0–12 h.3.5. 表面疏水性Fig. 5. Changes in ANS fluorescence spectra of Q and S after thermal treatment at pH 2.0 and 85 °C for 0–12 h.3.6 游离SH含量Fig. 6. Changes in free sulfhydryl groups content of Q and S after thermal treatment at pH 2.0 and 85 °C for 0–12 h.3.7. 荧光光谱法Fig. 7. Changes in fluorescence spectra of Q and S.3.8. 微观形貌Fig. 8. TEM micrographs of Q and S heated at pH 2.0 and 85 °C for 0 h, 2 h, 4 h, 8 h, 10 h, 12 h, respectively.3.9. 机制Fig. 9. Possible mechanism of peanut protein fibrils formation after hydration treatment at different pH.原文链接：https://doi.org/10.1016/j.foodhyd.2024.110599
