Key Lab of Meat Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, PR China.
Meat Sci. 2011 Mar;87(3):159-64. doi: 10.1016/j.meatsci.2010.10.001. Epub 2010 Oct 13.
Structural changes, textural properties and their relationships in pork myofibrillar proteins (PMP) were studied by Raman spectroscopy, texture profile analysis (TPA) and principal component analysis (PCA). Raman spectroscopy analysis revealed the occurrence of secondary structural changes in myofibrillar proteins. Modifications in the amide I (1600-1700 cm(-1)) and amide III (1200-1300 cm(-1)) regions indicated a significant (p<0.05) decrease in α-helix content, accompanied by a significant (p<0.05) increase in β-sheets, β-turns and random coil content. Texture property changes were also determined by TPA. All these features contributed to the formation of strong, irreversible heat-induced gels. The application of a dimensionality reducing technique such as PCA proved to be useful to determine the most influential properties of heat-induced gel. Significant (p<0.05) correlations were found between these structural changes and the textural characteristic (hardness) in the pork myofibrillar proteins system by PCA.
采用拉曼光谱、质构剖面分析（TPA）和主成分分析（PCA）研究了猪肉肌原纤维蛋白（PMP）的结构变化、质地特性及其关系。拉曼光谱分析显示肌原纤维蛋白发生了二级结构变化。酰胺 I（1600-1700 cm(-1)) 和酰胺 III（1200-1300 cm(-1)) 区域的修饰表明α-螺旋含量显著降低（p<0.05），同时β-折叠、β-转角和无规卷曲含量显著增加（p<0.05）。TPA 还确定了质地特性的变化。所有这些特征都促成了强的、不可逆的热诱导凝胶的形成。应用 PCA 等降维技术被证明有助于确定热诱导凝胶的最有影响的特性。通过 PCA 发现，这些结构变化与猪肉肌原纤维蛋白体系的质地特性（硬度）之间存在显著相关性（p<0.05）。
