Changes in secondary structure of myofibrillar protein and its relationship with water dynamic changes during storage of battered and deep-fried pork slices
Xi-Juan Guo, Heilongjiang Bayi Agricultural University, Daqing, China | Rui-Qi Wang, Heilongjiang Bayi Agricultural University, Daqing, China
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 alpha-helix and beta-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 (T₂₁) has a high negative correlation with a-helix, bsheet, and has a high positive correlation with irregular curl and beta-turn. The population of immobile water (P₂₂) has a very high positive correlation with alpha-helix, beta-sheet, and has a relatively high negative correlation with irregular curl and beta-turn. The immobilized water plays an important role in maintaining the secondary structure.
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