ArticleFood science and biotechnology2018
Changes in secondary structure of myofibrillar protein and its relationship with water dynamic changes during storage of battered and deep-fried pork slices.
Article in Food science and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Effects of polyphenolic compounds on the structure, allergenicity and gel properties of shrimp myofibrillar proteins.Journal of the science of food and agriculture · 2026Article
- Effect of Boiling Time on the Color, Water, Protein Secondary Structure, and Volatile Compounds of Beef.Foods (Basel, Switzerland) · 2025Article
- Optimizing Protein Profile, Flavor, Digestibility, and Microstructure: The Impact of Preheating and Reheating in Stir-Fried Chicken.Foods (Basel, Switzerland) · 2025Article
- Effects of deep frying and baking on the quality attributes, water distribution, and flavor characteristics of duck jerky.Frontiers in nutrition · 2024Article
- Biomolecules, Fatty Acids, Meat Quality, and Growth Performance of Slow-Growing Chickens in an Organic Raising System.Animals : an open access journal from MDPI · 2022Article
Corrections and comments
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Authors and funding
2 authors.
Funding
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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 (T
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