College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
Ultrason Sonochem. 2019 Jun;54:311-320. doi: 10.1016/j.ultsonch.2019.01.026. Epub 2019 Jan 22.
This study investigated the effect of ultrasound-assisted immersion freezing (UIF) at different ultrasonic power levels on the myofibrillar protein primary, secondary and tertiary structures of common carp (Cyprinus carpio). Furthermore, protein thermal stability, electrophoresis pattern, and microstructure of the muscle tissue were also studied. Compared with a control, an ultrasonic power of less than 175 W had no significant negative effect on protein primary structure (P > 0.05), including total sulfhydryl, reactive sulfhydryl, carbonyl groups, free amino groups, dityrosine content, and surface hydrophobicity. UIF at 175 W (UIF-175) minimized the changes in protein secondary and tertiary structures. There were no obvious changes in the SDS-PAGE patterns of the control and frozen sample proteins. Microstructure analysis showed that an appropriate ultrasonic power (UIF-175) promoted the formation of smaller and more uniform ice crystals, reduced the damage of muscle tissue by ice crystals, and maintained the sarcomere integrity. In addition, UIF-175 samples had higher protein thermal stability. Overall, ultrasound treatment at a proper power (UIF-175) effectively minimized the changes in protein structure and protected the protein thermal stability during freezing process.
本研究探讨了不同超声功率水平下超声辅助浸渍冻结（UIF）对鲤鱼（Cyprinus carpio）肌原纤维蛋白一级、二级和三级结构的影响。此外，还研究了肌肉组织的蛋白质热稳定性、电泳图谱和微观结构。与对照组相比，超声功率低于 175W 对蛋白质一级结构（P＞0.05）没有明显的负面影响，包括总巯基、反应性巯基、羰基、游离氨基、二酪氨酸含量和表面疏水性。在 175W 的超声功率下（UIF-175），蛋白质二级和三级结构的变化最小。对照组和冷冻样品蛋白质的 SDS-PAGE 图谱没有明显变化。微观结构分析表明，适当的超声功率（UIF-175）促进了更小且更均匀的冰晶形成，减少了冰晶对肌肉组织的损伤，并保持了肌节的完整性。此外，UIF-175 样品具有更高的蛋白质热稳定性。总体而言，适当功率（UIF-175）的超声处理有效地最小化了蛋白质结构的变化，并在冷冻过程中保护了蛋白质的热稳定性。
