Thermal Denaturation of Fish Myofibrillar Proteins
Summary
Fish myofibrillar proteins, primarily myosin and actin, form the contractile apparatus of muscle fibres and are key determinants of flesh texture, water‐holding capacity and gelation behaviour. Upon heating, these proteins undergo conformational transitions—loss of native secondary and tertiary structure—leading to exposure of hydrophobic regions, aggregation and network formation. The onset temperature and kinetics of denaturation vary by species, muscle type and ionic environment, directly influencing the sensory and functional properties of seafood products. Understanding thermal denaturation is crucial for optimising processing parameters in cooking, surimi production and canning, as well as for improving nutritional quality and shelf stability. Recent advances in calorimetry, spectroscopy and rheology have elucidated multistage unfolding events, providing a mechanistic basis for controlling texture and yield in industrial and domestic applications.
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Thermal Denaturation of Fish Myofibrillar Proteins publication trend
The graph below shows the total number of articles in thermal denaturation of fish myofibrillar proteins across all publications each year (not limited to Nature Index journals).
Technical terms
Myofibrillar proteins: The filamentous proteins (mainly myosin and actin) responsible for muscle contraction and key determinants of fish flesh texture.
Denaturation temperature (Td): The characteristic temperature at which a significant fraction of protein molecules loses native structure.
ATPase activity: Enzymatic function of myosin heads that hydrolyse ATP, loss of which indicates unfolding of the myofibrillar motor domain.
Thermal stability: The resistance of a protein’s native conformation to unfolding upon heating.
Gelation: Formation of a three‐dimensional protein network upon heating, affecting the firmness and water retention of processed fish products.
References
- Changes in ATPase Activities and Other Properties of Sardine Myofibrillar Proteins during Ice-storage. Nippon Suisan Gakkaishi (1980).
- Kinetic Analysis of the Thermal Inactivation Behavior of AMP Deaminase and IMPase in Each Muscle Type of Yellowtail Seriola quinqueradiata. Fishes (2025).
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