Physicochemical Dynamics of Myofibrillar Proteins in Frozen Storage

Freezing is widely employed to extend the shelf life of muscle foods, yet it provokes complex physicochemical transformations in myofibrillar proteins. Ice nucleation and growth impose mechanical stresses that disrupt the organised arrangement of myosin and actin filaments. Slow freezing and repeated freeze–thaw cycles intensify ice recrystallisation, driving protein unfolding, aggregation and oxidative modifications. As a result, water holding capacity diminishes, Ca2+-ATPase activity declines, surface hydrophobicity and carbonyl content rise, and gel strength and textural integrity are compromised. Changes in secondary and tertiary structures alter emulsifying properties and colour stability. Recent progress has centred on refining freezing kinetics, applying tailored cryoprotectants and harnessing novel technologies to stabilise protein conformation and functionality. These insights underpin strategies to mitigate quality loss, with significant ramifications for the global meat and seafood industries, from cold-chain logistics to consumer satisfaction.

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Physicochemical Dynamics of Myofibrillar Proteins in Frozen Storage publication trend

The graph below shows the total number of articles in physicochemical dynamics of myofibrillar proteins in frozen storage across all publications each year (not limited to Nature Index journals).

Technical terms

Myofibrillar proteins: Contractile proteins (myosin, actin) that determine muscle structure, gelation and water retention.

Cryoprotectant: Substance or additive that inhibits ice crystal growth and protein damage during freezing.

Ice recrystallisation: Growth of existing ice crystals into larger forms over time, disrupting cellular and protein structures.

Water holding capacity: The ability of proteins or gels to retain water when subjected to mechanical or thermal stress.

Protein denaturation: Loss of native secondary and tertiary structure due to physical or chemical stress, impairing functionality.

References

1. Effects of phosphorylated ovalbumin on the quality of pork myofibrillar protein gel: an insight into gelling and physicochemical properties. Journal of Future Foods (2024).
2. Effects of single-, dual-, and multi-frequency ultrasound-assisted freezing on the muscle quality and myofibrillar protein structure in large yellow croaker (Larimichthys crocea). Food Chemistry X (2022).
3. Ultrasonic Freezing Reduces Protein Oxidation and Myofibrillar Gel Quality Loss of Common Carp (Cyprinus carpio) during Long-Time Frozen Storage. Foods (2021).