油炸肉片贮藏过程中肌原纤维蛋白二级结构变化及其与水分动态变化的关系
Changes in secondary structure of myofibrillar protein and its relationship with water dynamic changes during storage of battered and deep-fried pork slices.
作者信息
Guo Xi-Juan, Wang Rui-Qi
机构信息
College of Food Science, Heilongjiang Bayi Agricultural University, Daqing, 163319 China.
出版信息
Food Sci Biotechnol. 2018 May 23;27(6):1667-1673. doi: 10.1007/s10068-018-0395-0. eCollection 2018 Dec.
Fourier transform infrared spectroscopy was used to analyze the changes of secondary structure of myofibrillar proteins in short-term storage of battered and deep-fried pork slices. These changes were combined with low-field NMR analysis results to analyze the correlation between secondary structure and dynamic changes of water content. The results showed that the number of α-helix and β-sheet decreased by 22.90 and 16.54% respectively, and the orderly structure changed to the disorder structure. The correlation results show that NMR spin-spin relaxation time (T) has a high negative correlation with α-helix, β-sheet, and has a high positive correlation with irregular curl and β-turn. The population of immobile water (P) has a very high positive correlation with α-helix, β-sheet, and has a relatively high negative correlation with irregular curl and β-turn. The immobilized water plays an important role in maintaining the secondary structure.
采用傅里叶变换红外光谱法分析了 battered 和油炸猪肉片短期储存过程中肌原纤维蛋白二级结构的变化。将这些变化与低场核磁共振分析结果相结合，分析二级结构与水分动态变化之间的相关性。结果表明，α-螺旋和β-折叠的数量分别减少了22.90%和16.54%，有序结构转变为无序结构。相关性结果表明，核磁共振自旋-自旋弛豫时间（T）与α-螺旋、β-折叠呈高度负相关，与不规则卷曲和β-转角呈高度正相关。不可移动水的含量（P）与α-螺旋、β-折叠呈非常高的正相关，与不规则卷曲和β-转角呈相对较高的负相关。固定化水在维持二级结构中起着重要作用。
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