【摘要】 为深入了解酱牛肉加工过程中蛋白质结构变化，借助酶标仪、扫描电子显微镜、傅里叶红外光谱仪、核磁共振分析仪等设备，以蛋白浊度、分子间相互作用力、微观结构、二级结构变化和水分分布为指标，对酱牛肉加工过程中（原料、滚揉腌制、卤制）和不同温度二次杀菌（90、100、110、120℃）的样品进行分析。结果：酱牛肉样品中提取的肌原纤维蛋白浊度高于肌浆蛋白浊度，滚揉腌制可显著降低肌浆蛋白和肌原纤维的蛋白浊度（P<0.05），热处理使蛋白浊度升高；滚揉腌制提高了蛋白质分子间相互作用力，热处理降低了蛋白质分子间静电相互作用，氢键、疏水相互作用和二硫键是样品中主要分子间作用力；不同加工处理对样品中肌浆蛋白和肌原纤维蛋白的结构均有破坏，随加工工艺增多（滚揉腌制、卤制、二次杀菌）破坏程度增大，且二次杀菌温度越高，蛋白质结构破坏越严重；滚揉腌制、卤制、二次杀菌对蛋白质二级结构有明显影响；二次杀菌酱牛肉样品中，经100℃杀菌后自由水含量和总水分含量最高，不同杀菌温度对束缚水含量的影响不显著（P>0.05）。更多还原

【Abstract】 In order to understand the changes of protein structure during the processing of spiced beef, protein turbidity,intermolecular interactions, microstructure, secondary structure and water distribution of samples collected at different stages of processing(raw meat, tumble marination, cooking, and secondary sterilization at 90, 100, 110 or 120 ℃) were detected by a microplate reader, a scanning electron microscope, a Fourier transform infrared spectrometer, and a nuclear magnetic resonance analyzer. Results showed that the turbidity of myofibrillar protein extracted from spiced beef was higher than that of sarcoplasmic protein. Tumble marination reduced the turbidity of sarcoplasmic and myofibrillar protein(P < 0.05),whereas heat treatment had the opposite effect. Tumble marination increased the protein-protein interactions, while heat treatment reduced the electrostatic interaction between protein molecules. Hydrogen bond, hydrophobic interaction and disulfide bond were the main intermolecular interaction forces. Different treatments destroyed the structures of sarcoplasmic and myofibrillar protein,and the degree of damage increased with increasing number of processing steps and increasing secondary sterilization temperature.Tumble marination, cooking and secondary sterilization had significant effects on the secondary structure of proteins, the free water content and total water content were the highest after sterilization at 100 ℃ among the four temperatures, and the effect of different sterilization temperatures on the bound water content was not significant(P > 0.05).更多还原