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Updated: Jul 12, 2026

Lipid-Protein Membrane Structure-Function Characterization using Droplet Interface Bilayers
Published on: June 12, 2026
Modulating interfacial adsorption and lipid stability in myofibrillar protein-soy protein isolate emulsion gels:
Zhifeng Tan1, Xiaoqing Yang1, Feiyang Li1
1State Key Laboratory of Marine Food Processing and Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, Liaoning, China.
None:
This study elucidated the molecular mechanisms by which polyphenol structure regulates the stability of myofibrillar protein (MP)-soy protein isolate (SPI) complex emulsion gels. The construction of the complex protein improved protein dispersion and emulsifying performance. Gallic acid (GA) and taxifolin (TF) further promoted interfacial adsorption and film formation at the oil-water interface. In particular, the TF-modified system exhibited higher interfacial viscoelasticity and adsorption stability, facilitating the unfolding and rearrangement of interfacial protein. Molecular dynamics simulation showed that TF-modified complexes formed a continuous viscoelastic interfacial film with a thickness of 2.08 nm, markedly higher than the 0.94 nm film formed by pure MP. This contributed to oil droplet dispersion, interfacial film integrity, and lipid retention. In contrast, epigallocatechin gallate (EGCG) may induce excessive aggregation of interfacial protein owing to its larger molecular size and multipoint binding capacity, thereby weakening interfacial film stability and impairing oil-retention capacity.
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