Changes in secondary structure of myofibrillar protein and its relationship with water dynamic changes during storage of battered and deep-fried pork slices.

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 α-helix and β-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 α-helix, β-sheet, and has a high positive correlation with irregular curl and β-turn. The population of immobile water (P22) has a very high positive correlation with α-helix, β-sheet, and has a relatively high negative correlation with irregular curl and β-turn. The immobilized water plays an important role in maintaining the secondary structure.