Functional Properties of Aquatic Muscle Proteins
Summary
Aquatic muscle proteins, predominantly myofibrillar proteins such as myosin and actin, underpin both the structural integrity and the functional characteristics of fish and shellfish muscle. These proteins confer contractile strength, viscoelastic behaviour and water‐holding capacity, all of which influence texture, juiciness and processing performance in seafood products. Accessory proteins including paramyosin, tropomyosin and structural filament proteins modulate filament assembly and contribute to gelation and network formation under thermal or ionic induction. The stability of these proteins under varying salinity, pH and temperature conditions determines their susceptibility to denaturation, aggregation or proteolytic degradation during storage, freezing and cooking. Functional attributes such as gel strength, cohesiveness, emulsion stability and cryostability are critical for applications ranging from surimi and gel‐based feeds to frozen‐thawed fillets. Understanding the molecular interactions—hydrophobic, electrostatic and covalent cross-links—that govern protein solubility and network formation is essential for optimising product quality, shelf life and nutritional value in global aquaculture and seafood industries.
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Functional Properties of Aquatic Muscle Proteins publication trend
The graph below shows the total number of articles in functional properties of aquatic muscle proteins across all publications each year (not limited to Nature Index journals).
Technical terms
Myofibrillar proteins: Contractile proteins, primarily myosin and actin, that form the filamentous structures responsible for muscle contraction and gel network formation.
Paramyosin: A thick‐filament protein found in invertebrate muscle that contributes to gel strength and viscoelasticity through salt-dependent self‐assembly.
Gelation: The process by which soluble proteins aggregate and form a three-dimensional network, resulting in a viscoelastic gel.
Cryoprotectant: A substance, often low-molecular-mass compounds, that inhibits ice crystallisation and protein denaturation during freezing.
Water-holding capacity: The ability of muscle proteins to retain water under applied forces or during processing, affecting juiciness and yield.
References
- Moving towards Gel for Fish Feeding: Focus on Functional Properties and Its Acceptance. Gels (2023).
- The influence of KCl concentration on the gelation of myofibrillar protein giant squid (Dosidicus gigas) due to molecular conformation change. Frontiers in Nutrition (2023).
- Partial Characterization of a Low-Molecular-Mass Fraction with Cryoprotectant Activity from Jumbo Squid (Dosidicus gigas) Mantle Muscle. Food Technology and Biotechnology (2019).
- Biochemical and physicochemical characteristics of the major muscle proteins from fish and shellfish. Fisheries Science (2020).
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