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Updated: Apr 6, 2026

Tissue Triage and Freezing for Models of Skeletal Muscle Disease
Published on: July 15, 2014
Freeze-thaw induced structural destabilization and oxidation of beef myofibrillar proteins: evidence from experiments
Yingying Zhu1, Jiaying Zhu1, Qian Li2
1Department of Food Nutrition and Test, Suzhou Polytechnic University, Suzhou, Jiangsu, China; State Key Laboratory of Meat Quality Control and Cultured Meat, Key Laboratory of Meat Processing, Jiangsu Synergetic Innovation Center of Meat Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
Abstract:
Repeated freeze-thaw (F-T) cycles are commonly present under cold chain conditions, degrade beef quality by damaging myofibrillar proteins (MPs). This study combined physicochemical analysis and molecular dynamics (MD) simulations to investigate the effects of repeated (0, 1, 3, 5 and 7) F-T cycles on structural and physicochemical properties of MPs in beef. Results demonstrated that repeated F-T cycles induced significant denaturation and oxidation of MPs, as evidenced by α-helix content dropped from 32.33% to 28.65%, random coils rose from 35.53% to 40.28% (P < 0.05), and sulfhydryl group decreased from 17.24 nmol/mg to 15.20 nmol/mg MPs. MD simulations revealed myosin destabilization via disrupted hydrogen bonds and hydrophobic exposure. Key sensitive residues lysine and arginine in myosin head were identified, while the conformation of myosin tail was more seriously damaged by F-T. Protein aggregation and oxidative modifications collectively explained quality deterioration. Limiting F-T cycles to ≤3 was recommended for quality preservation.
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