Ultrasound-Assisted Modulation of Myofibrillar Protein Properties
Summary
Ultrasound-assisted modulation has emerged as a versatile, non-chemical approach to tailor the physicochemical and functional attributes of myofibrillar proteins. Through the application of high-intensity sound waves, cavitation events generate localised shear forces and transient micro-jets that induce molecular unfolding, expose reactive residues, and promote controlled aggregation or cross-linking. These structural modifications enhance solubility, emulsification, gelation and rheological behaviour, offering precise control over particle size, surface hydrophobicity and network formation. Both continuous-flow and batch sonication systems can be tuned by frequency, power and duration, enabling adaptation to a wide range of protein sources—from fish and poultry to red meat. The approach addresses industry demands for clean-label processing, reduced chemical additives and energy efficiency. By improving oxidative stability and textural properties, ultrasound treatment has significant potential in value-added food formulations, sustainable utilisation of by-products and the development of novel protein-based materials with tailored functional performance.
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Ultrasound-Assisted Modulation of Myofibrillar Protein Properties publication trend
The graph below shows the total number of articles in ultrasound-assisted modulation of myofibrillar protein properties across all publications each year (not limited to Nature Index journals).
Technical terms
Cavitation: The formation and collapse of vapor bubbles in a liquid under ultrasonic pressure, generating shear forces.
Surface hydrophobicity: A measure of exposed non-polar regions on a protein surface, influencing interfacial interactions.
Sulfhydryl group: A thiol (–SH) functional group in cysteine residues that contributes to protein folding and cross-linking.
Zeta potential: The electrical potential at the slipping plane of particles in suspension, indicating colloidal stability.
Myofibrillar proteins: The salt-soluble muscle proteins (e.g. myosin, actin) responsible for texture and mechanical properties in meat.
References
- High-intensity ultrasound modified the functional properties of Neosalanx taihuensis myofibrillar protein and improved its emulsion stability. Ultrasonics Sonochemistry (2023).
- Effects of Ultrasound-Assisted Emulsification on the Emulsifying and Rheological Properties of Myofibrillar Protein Stabilized Pork Fat Emulsions. Foods (2021).
- Influence of Multi-Frequency Ultrasound Treatment on Conformational Characteristics of Beef Myofibrillar Proteins with Different Degrees of Doneness. Foods (2023).
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