The application of dynamic high-pressure microfluidization (DHPM) provides interesting modifications in food structures. However, the effects of DHPM on the structural and rheological properties of rapeseed protein isolate (RPI) were scarcely investigated. In this study, the average hydrodynamic size of RPI treated by DHPM significantly declined from 239.2 nm to 170 nm with the pressure and time rising to 60 MPa and 2 min. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis found that DHPM did not affect the molecular mass of the RPI. The changes in the intrinsic fluorescence and circular dichroism spectra showed that tertiary and secondary structures of RPI were altered, as proved by the higher fluorescence intensity and greater conversion of random coils and β-sheets into α-helices compared with the control (unprocessed RPI). The spatial unfolding of the RPI structure and the dissociation of chemical bonds influenced its rheological behavior. All RPI suspensions (15%, w/v) processed by DHPM had lower apparent viscosity, moduli, higher gelling temperature (up to 69.7 °C) than control, and the differences in rheological performance were closely dependent on the treatment pressure and time. In conclusion, through this study of the effects of DHPM on RPI, DHPM was shown to be a potential method for modifying proteins and reducing the consistency of high-protein fluid foods.

动态高压微流化 (DHPM) 的应用对食物结构进行了有趣的修改。然而，DHPM 对油菜籽分离蛋白 (RPI) 的结构和流变特性的影响几乎没有被研究过。在这项研究中，DHPM 处理的 RPI 的平均流体动力学尺寸从 239.2 nm 显着下降到 170 nm，压力和时间上升到 60 MPa 和 2 分钟。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析发现DHPM不影响RPI的分子量。固有荧光和圆二色光谱的变化表明 RPI 的三级和二级结构发生了改变，与对照（未处理的 RPI）相比，荧光强度更高，无规卷曲和 β-折叠更多地转化为 α-螺旋证明了这一点. RPI结构的空间展开和化学键的解离影响其流变行为。所有 RPI 暂停（15%，w / v ) DHPM处理的表观粘度、模量、胶凝温度(高达69.7°C)均低于对照，流变性能的差异与处理压力和时间密切相关。总之，通过对 DHPM 对 RPI 影响的研究，DHPM 被证明是一种潜在的改变蛋白质和降低高蛋白流质食品稠度的方法。