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Updated: Jun 25, 2026

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
From protein structural reconfiguration to long-term emulsion stabilization: How ultrasound-microwave synergistic
Yufeng Chen1, Siqi Lan1, Jipeng Gu1
1College of Food Science and Technology, College of Chemical Engineering, Zhejiang University of Technology, Hangzhou 310014, China; Key Laboratory of Green, Low-carbon and Efficient Development of Marine Fishery Resources, Hangzhou 310014, China.
Abstract:
The application of native myofibrillar protein (MP)-stabilized emulsions is limited by salt dependence and poor stability. This study investigated the effects of ultrasound (U-MP), microwave (M-MP), and combined (UM-MP) treatments on MP under no-added-salt conditions. UM-MP significantly reduced particle size (to 537.76 nm), increased surface hydrophobicity (11.093 μg/mg), and shifted secondary structure from α-helix to β-sheet and random coil, resulting in high interfacial adsorption (92.37 ± 2.01%). The UM-MP emulsion showed excellent storage stability with no phase separation after 72 h. This stabilization was attributed to the synergistic effects of ultrasound-induced cavitation and microwave-induced unfolding, which generated restructured nanoscale MP aggregates capable of rapid interfacial coverage. A dual mechanism of mechanical barrier reinforcement and viscoelastic network formation effectively suppressed droplet coalescence. These findings provide an effective strategy for designing a no-added-salt and MP-stabilized emulsion suitable for functional food formulations.
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