1. Interpretation and rapid detection of secondary structure modification of actomyosin during frozen storage by near-infrared hyperspectral imaging.
- Author
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Cheng, Weiwei, Sun, Da-Wen, Pu, Hongbin, and Wei, Qingyi
- Subjects
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ACTOMYOSIN , *HYPERSPECTRAL imaging systems , *STATISTICAL correlation , *RADIANT intensity , *ALIPHATIC compounds - Abstract
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 R2 CV 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. Highlights • NIR HSI was employed by the first time to monitor α-helix fraction of actomyosin. • G2D-CS was used for understanding the process of secondary structure modification. • H2D-CS was applied for identifying α-helix related NIR wavebands. • PLSR model built by the selected wavebands showed good results. [ABSTRACT FROM AUTHOR]
- Published
- 2019
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