School of Food Science and Technology, Key Laboratory of Carbohydrate Chemistry and Biotechnology Ministry of Education, Jiangnan University, Lihu Road 1800, Wuxi 214122, China; National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Lihu Road 1800, Wuxi 214122, China; Jiangsu Provincial Research Center for Bioactive Product Processing Technology, Jiangnan University, Lihu Road 1800, Wuxi 214122, China.
School of Food Science and Technology, Key Laboratory of Carbohydrate Chemistry and Biotechnology Ministry of Education, Jiangnan University, Lihu Road 1800, Wuxi 214122, China; National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Lihu Road 1800, Wuxi 214122, China; Jiangsu Provincial Research Center for Bioactive Product Processing Technology, Jiangnan University, Lihu Road 1800, Wuxi 214122, China.
Food Chem. 2021 Aug 30;354:129554. doi: 10.1016/j.foodchem.2021.129554. Epub 2021 Mar 11.
The rice glutelin fibrils (RGFs) were formed under heating at acidic condition, and the optimal condition was achieved at pH 2, 150 mM (ionic strength), 4% (protein concentration), 90 °C and 300 rpm (stirring speed) through the thioflavin T intensity. The atomic force microscopy images showed that the average contour length of RGFs increased from < 100 to 365 nm under the optimal fibrillation. The average particle size of rice glutelin (RG) decreased from 650 to 221 nm after initial heating time. Combining the degraded subunits, it suggested that RG was hydrolyzed to peptides, then these released peptides assembled into the ordered fibrils via intermolecular interactions, accompanying by the structural rearrangement. Additionally, the foaming and emulsifying properties were improved during fibrillation, which could be related to the interfacial properties and structure of RGFs. This work will deepen the understanding of the formation of RGFs and explore their potential application.
大米谷蛋白纤维(RGFs)在酸性条件下加热形成,通过硫代黄素 T 强度,在 pH 2、150 mM(离子强度)、4%(蛋白质浓度)、90°C 和 300 rpm(搅拌速度)下达到最佳条件。原子力显微镜图像显示,在最佳纤化条件下,RGFs 的平均轮廓长度从 <100nm 增加到 365nm。初始加热后,大米谷蛋白(RG)的平均粒径从 650nm 减小到 221nm。结合降解的亚基,表明 RG 被水解成肽,然后这些释放的肽通过分子间相互作用组装成有序的纤维,伴随着结构重排。此外,在纤化过程中起泡和乳化性能得到提高,这可能与 RGFs 的界面性质和结构有关。这项工作将加深对 RGFs 形成的理解,并探索其潜在的应用。