Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
