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Updated: May 13, 2026

The Mechanics of (Poro-)Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton
Published on: March 10, 2023
Low kinetic perturbation by the rapidly advancing ice-water interface suppresses Na+/Cl- induced myofibrillar protein
Yajin Zhang1, Ziaur Rahman1, Hongwei Song1
1College of Food Science and Technology, Huazhong Agricultural University/National R and D Branch Center for Conventional Freshwater Fish Processing (Wuhan), Wuhan, Hubei Province 430070, PR China; Key Laboratory of Environment Correlative Dietology, Ministry of Education, Huazhong Agricultural University, Wuhan, Hubei Province 430070, PR China.
Abstract:
Protein aggregation control remains a key challenge in industrial freezing processes. This study investigated the effect of the formation and migration of the ice-water interface on stability of myofibrillar proteins (MP) in brined fish flesh. Freezing treatments at -35 °C and - 110 °C were applied to modulate ice-water interface migration and its impact on MP properties. Slow migration promoted myofibrillar network assembly via hydrophobic interactions, whereas rapid migration trapped salt ions and MP within ice crystals, reducing protein interactions and surface hydrophobicity while preserving native conformation. However, this process may separate soluble proteins and filaments. Molecular dynamics simulations showed that freezing destabilizes the myosin head region (residues 343-449). Rapid freezing immobilized ions and MP in ice, while optimal salt content (1.00%) increased unfreezable water, weakening ice-protein electrostatic energy. Rapid interface migration compacted proteins. These findings establish a new paradigm for preserving protein integrity in frozen foods through controlled ice crystallization.
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