Gelation Mechanisms of Myofibrillar Proteins in Food Systems

Myofibrillar proteins, principally myosin and actin, underpin the formation of gel networks in muscle‐based food products. Upon heating or chemical modification, these proteins undergo unfolding and intermolecular association driven by hydrophobic interactions, disulfide bond formation and electrostatic forces. Partial conversion of α-helices into β-sheets exposes reactive side chains, allowing formation of a continuous three-dimensional network that entraps water and fat. The gel strength and water-holding capacity depend on factors such as ionic strength, pH, protein concentration and the presence of polysaccharides or alternative proteins. Fine‐tuning these parameters enables control of texture, juiciness and stability in processed meats, plant–animal hybrid products and novel protein formulations. Advances in spectroscopic and rheological techniques have elucidated the dynamic evolution of protein aggregates, from initial nucleus formation through network maturation. Practical applications range from low-phosphate clean-label sausages to surimi enhancement and inclusion of sustainable protein sources. A growing focus is the design of gels with targeted functionalities, such as reduced cooking loss, tailored bite and improved shelf life, addressing both industrial processing demands and consumer preferences globally.

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Technical terms

Gelation: The process by which proteins unfold and associate to form a semisolid three-dimensional network.

Myofibrillar proteins: Muscle proteins, chiefly myosin and actin, responsible for contraction and gel formation when heated or modified.

Hydrophobic interaction: Association of non-polar amino acid side chains that drives protein aggregation in aqueous environments.

Disulfide bond: Covalent linkage between cysteine residues that stabilises protein networks upon oxidation or heating.

Water-holding capacity: The ability of a gel network to retain bound water against external pressures or during cooking.

Rheology: The study of flow and deformation of materials, often quantified by storage modulus (G′) and loss modulus (G″) in gels.

References

1. Porcine myofibrillar protein gel with edible insect protein: Effect of pH-shifting. LWT (2022).
2. Relationship between Molecular Structure and Heat-Induced Gel Properties of Duck Myofibrillar Proteins Affected by the Addition of Pea Protein Isolate. Foods (2022).
3. Phosphate Elimination in Emulsified Meat Products: Impact of Protein-Based Ingredients on Quality Characteristics. Foods (2021).