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Heat-induced evolution of myosin aggregation patterns: The role in regulating interfacial layer lateral-longitudinal
Li Hu1, Yanwei Zhang1, Zhichao Xiao2
1College of Food Science, Shenyang Agricultural University, Shenyang 110866, China.
Food Chemistry
|November 5, 2025
Summary
Mild preheating of myosin affects its aggregation, influencing emulsifying activity. Partially unfolded myosin monomers enhance oil-in-water emulsion stability through improved flexibility and surface hydrophobicity.
Area of Science:
- Food Science
- Protein Chemistry
- Colloid Science
Background:
- Myosin's conformational changes and aggregation are critical for its interfacial behavior.
- Understanding these changes is key to controlling food emulsion properties.
Purpose of the Study:
- To investigate the impact of mild preheating on myosin aggregation.
- To correlate myosin's structural evolution with its emulsifying and emulsion stabilizing capabilities.
- To elucidate the role of intermolecular interactions in myosin-stabilized emulsions.
Main Methods:
- Mild preheating of myosin at varying temperatures (40-55 °C).
- Characterization of myosin aggregation states (monomers, oligomers, aggregates).
- Assessment of emulsifying activity and emulsion stability in oil-in-water systems.
- Analysis of interfacial layer viscoelasticity and emulsion shear viscosity.
Main Results:
- Three myosin aggregation patterns were observed: native monomers/soluble oligomers, partially unfolded monomers, and irreversible aggregates.
- Intermolecular interactions in soluble oligomers and partially unfolded monomers were primarily non-covalent.
- Enhanced emulsifying activity correlated with increased conformational flexibility and surface hydrophobicity, not aggregate size.
- Emulsions stabilized by partially unfolded myosin monomers showed superior stability (98.38 ± 10.57%).
Conclusions:
- Myosin's interfacial adsorption and emulsifying properties are dictated by its intermolecular interactions and conformational flexibility.
- Partially unfolded myosin monomers offer optimal properties for stabilizing oil-in-water emulsions.
- This research provides insights for enhancing the quality of emulsified meat products through controlled protein modification.
Keywords:
Aggregation evolutionInterfacial propertiesMyosinNon-covalent interactionsStructure-function relationshipMore Related Videos
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