Myofibrillar Protein Modification and Functional Characterization

Myofibrillar proteins, principally myosin and actin, form the structural framework of muscle and underpin many desirable textural and functional attributes in meat and fish products. Modifying these proteins through physical, chemical or enzymatic means allows control over solubility, gelation, emulsification and foaming, thereby tailoring food structure, mouthfeel and stability. Common approaches include pH-shifting to induce controlled unfolding and refolding, glycosylation or protein–polysaccharide conjugation to enhance stability, high-intensity ultrasound to alter molecular assembly, and high-pressure or thermal treatments to modulate protein solubility. Functional characterisation employs techniques such as rheometry, spectroscopy, differential scanning calorimetry and microscopy to quantify changes in secondary structure, particle size, surface hydrophobicity and interfacial properties. These modifications support healthier, lower-salt and plant-based or upcycled protein formulations, advancing both traditional meat processing and novel protein platforms in response to sustainability and consumer health trends.

Research from Nature Portfolio

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Research from all publishers

Recent studies have illustrated how specific sugars and polysaccharides can markedly improve emulsion quality by forming electrostatic and hydrogen-bonded complexes with myofibrillar proteins. For example, incorporation of a heteropolysaccharide during oil-in-water emulsification reduced droplet size, increased negative surface charge and enhanced long-term stability, demonstrating a route to cleaner-label emulsifiers. In parallel, the combination of pH-shifting and high-intensity ultrasound has been shown to restore functional properties of structurally compromised chicken breast proteins. Ultrasound applied during the unfolding stage promotes exposure of hydrophobic groups and conversion of α-helices to β-sheets, leading to superior solubility, emulsification and gel strength, whereas ultrasound during refolding can impede ordered assembly. Advancing applications in low-salt meat analogues, divalent cations such as calcium and magnesium have been paired with ultrasound to create Pickering emulsions stabilised by myofibrillar microgels. These cations increase electrostatic repulsion and reduce microgel particle size, yielding highly uniform, stable emulsions under reduced-salt conditions. Collectively, these diverse modification strategies highlight the interplay between molecular conformation, interfacial phenomena and macroscopic functional performance, offering paths to healthier and more sustainable protein ingredients.

Myofibrillar Protein Modification and Functional Characterization publication trend

The graph below shows the total number of articles in myofibrillar protein modification and functional characterization across all publications each year (not limited to Nature Index journals).

Technical terms

Myofibrillar proteins: Contractile proteins, chiefly myosin and actin, that give muscle its structural integrity and functional versatility.

Glycosylation: Covalent attachment of carbohydrate moieties to protein, often improving stability and solubility.

pH-shifting: Controlled denaturation and refolding of proteins by transient exposure to acidic or alkaline pH.

High-intensity ultrasound: Acoustic energy treatment that induces cavitation, leading to protein unfolding and particle size reduction.

Pickering emulsion: Emulsion stabilised by solid colloidal particles rather than conventional surfactants.

Zeta potential: Electrical potential at the particle–liquid interface, reflecting surface charge and colloidal stability.

Surface hydrophobicity: Extent of nonpolar residues exposed on a protein’s surface, influencing interactions at interfaces.

References

1. The physicochemical properties and stability of myofibrillar protein oil-in-water emulsions as affected by the structure of sugar. Food Chemistry X (2023).
2. Synergistic effect of high-intensity ultrasound and pH-shifting on the functionalities of chicken wooden breast myofibrillar protein: Reveal the mechanism of protein structure change. LWT (2023).
3. Effect of Combined High Pressure and Thermal Treatment on Myofibrillar Proteins Solubilization of Beef Muscle. International Journal of Molecular Sciences (2011).
4. Having their cake and eat it too: Effects of different cations in reduced-salt myofibrillar protein microgel pickering emulsion under high-intensity ultrasound. LWT (2024).