4.7 Article

Interpretation and rapid detection of secondary structure modification of actomyosin during frozen storage by near-infrared hyperspectral imaging

Journal

JOURNAL OF FOOD ENGINEERING
Volume 246, Issue -, Pages 200-208

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.jfoodeng.2018.10.029

Keywords

Hyperspectral imaging; Actomyosin; Secondary structure; alpha-helix fraction; Two-dimensional correlation spectroscopy

Funding

  1. National Key R&D Program of China [2017YFD0400404]
  2. Collaborative Innovation Major Special Projects of Guangzhou City [201604020007, 201604020057]
  3. Guangdong Provincial Science and Technology Plan Projects [2015A020209016, 2016A040403040]
  4. National Key Technologies RD Program [2015BAD19B03]
  5. Natural Science Foundation of Guangdong Province [2017A030310558]
  6. China Postdoctoral Science Foundation [2017M612672]
  7. Fundamental Research Funds for the Central Universities [2017MS067, 2017M5075]
  8. Agricultural Development and Rural Work of Guangdong Province [2017LM4173]
  9. S&T Project of Guangdong Province [2017B020207002]
  10. Pearl River S&T Nova Program of Guangzhou [201610010104]
  11. Hong Kong - Macau - Taiwan Collaborative Innovation Platform of Guangdong Province on Intelligent Food Quality Control and Process Technology Equipment [2015KGJHZ001]
  12. Guangdong Provincial R&D Centre for the Modern Agricultural Industry on Non-destructive Detection and Intensive Processing of Agricultural Products
  13. Common Technical Innovation Team of Guangdong Province on Preservation and Logistics of Agricultural Products [2016LM2154]
  14. Innovation Centre of Guangdong Province for Modern Agricultural Science and Technology on Intelligent Sensing and Precision Control of Agricultural Product Qualities

Ask authors/readers for more resources

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 alpha-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 R-CV(2) of 0.836 in predicting a-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.

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