Abstract Secondary structure of proteins is closely related to the overall quality of meat. The sequence of the changes in chemical bonds caused by secondary structure modification and rapid detection method of secondary structure fractions was investigated by near-infrared hyperspectral imaging combined with generalized (G2D-CS) and heterospectral (H2D-CS) two-dimensional correlation analysis in this study. Synchronous and asynchronous spectral results from G2D-CS analysis indicated that, as α-helix fraction decreasing, the spectral intensity of N H stretching changed before that of the C H and O H, and the spectral fluctuation of O H stretching occurred after the carbonyl related C H band and before those aliphatic and aromatic C H band. Feature wavebands identified by H2D-CS analysis obtained good results with R2CV of 0.836 in predicting α-helix fractions. The results of this study are useful for interpreting the secondary structure modification process of proteins during frozen storage and monitoring the secondary structure fraction in a rapid way.

中文翻译：

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近红外高光谱成像解读及快速检测冻存过程中肌动球蛋白二级结构修饰

摘要 蛋白质的二级结构与肉类的整体品质密切相关。通过近红外高光谱成像结合广义（G2D-CS）和异谱（H2D-CS）二维相关分析，研究了二级结构修饰引起的化学键变化的顺序和二级结构馏分的快速检测方法。这项研究。G2D-CS分析的同步和异步光谱结果表明，随着α-螺旋分数的减少，NH伸缩的光谱强度先于CH和OH的光谱强度发生变化，而OH伸缩的光谱波动发生在羰基相关的CH带和在那些脂肪族和芳香族 CH 带之前。通过 H2D-CS 分析识别的特征波段在 R2CV 为 0 时获得了良好的结果。836 在预测 α-螺旋分数。本研究的结果有助于解释蛋白质在冷冻储存过程中的二级结构修饰过程并快速监测二级结构分数。