Gao Ruichang, Feng Xueping, Li Wenwen, Yuan Li, Ge Jing, Lu Daoli, Chen Bin, Yu Gang
2School of Food and Biological Engineering, Jiangsu University, Zhenjiang, 212013 China.
1South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou, 510300 China.
Food Sci Biotechnol. 2016 Feb 29;25(1):21-26. doi: 10.1007/s10068-016-0003-0. eCollection 2016.
Changes in white shrimp () protein during thermal denaturation were studied using Raman spectroscopy and isotopic H/D exchange. Denaturation of shrimp protein began after heating for 10 min at 50°C. A decrease in the percentage of α-helices accompanied by an increase in the percentage of β-sheets occurred while the total percentage of disordered structures increased. With extension of the exchange time, the relative intensity of the O-D bond increased, accompanied by a higher relative O-D bond intensity for heated shrimp, compared with unheated shrimp. H/D exchange revealed a higher rate of deuteration kinetics in heated shrimp than for unheated shrimp, especially during the first 2 h, consistent with water loss from denatured white shrimp protein. Physical property changes in muscle tissue can be caused by changes in hydrogen bonding and hydrophobicity during thermal processes.
利用拉曼光谱和同位素H/D交换研究了凡纳滨对虾（）蛋白质在热变性过程中的变化。虾蛋白在50°C加热10分钟后开始变性。α-螺旋百分比降低，同时β-折叠百分比增加，无序结构的总百分比增加。随着交换时间的延长，O-D键的相对强度增加，与未加热的虾相比，加热虾的O-D键相对强度更高。H/D交换显示，加热虾的氘化动力学速率高于未加热的虾，尤其是在最初2小时内，这与变性凡纳滨对虾蛋白质的水分流失一致。热过程中氢键和疏水性的变化可导致肌肉组织的物理性质改变。
