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

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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.

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Acknowledgements

Heilongjiang Bayi Agricultural University Dr. research fund.

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  1. College of Food Science, Heilongjiang Bayi Agricultural University, Daqing, 163319, China

    Xi-Juan Guo & Rui-Qi Wang

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  1. Xi-Juan Guo
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  2. Rui-Qi Wang
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Correspondence to Xi-Juan Guo.

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Guo, XJ., Wang, RQ. Changes in secondary structure of myofibrillar protein and its relationship with water dynamic changes during storage of battered and deep-fried pork slices. Food Sci Biotechnol 27, 1667–1673 (2018). https://doi.org/10.1007/s10068-018-0395-0

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  • DOI: https://doi.org/10.1007/s10068-018-0395-0

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