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Peer-reviewedCC BY 4.0Molecules

Ultrasound-Driven Conformational Rearrangement of Coilia ectenes taihuensis Myofibrillar Protein Enhances Emulsion Stability

  • Xinhui Zhou1
  • Zhangyan Sun1
  • Lijun Zhu1
  • Suting Zhuang1
  • Xiu Wang2
  • Changjun Zhu3
  • Mingfeng Xu1
  1. 1Zhejiang Provincial Modern Biology and Medicine Industry College, College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou 311121, China
  2. 2School of Advanced Materials Engineering, Jiaxing Nanhu University, Jiaxing 314001, China
  3. 3College of Biological and Chemical Engineering, Jiaxing University, Jiaxing 314001, China
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Abstract

Myofibrillar protein (MP) from Coilia ectenes taihuensis (CMP) has potential as a natural emulsifier; however, its relatively compact native structure may restrict its functional performance. This study evaluated the effects of ultrasound treatment (0–600 W) on CMP conformational characteristics and the stability of CMP-based emulsions. Ultrasound-induced power-dependent structural and oxidative modifications in CMP, as evidenced by increased carbonyl content, decreased sulfhydryl content, secondary structure rearrangement, and altered surface hydrophobicity. Under the conditions tested, CMP treated at 450 W exhibited the highest surface hydrophobicity and enhanced solubility, which were associated with improved emulsifying properties. The emulsifying activity index increased from 39.93 m2/g to 82.17 m2/g, accompanied by reduced droplet size, higher absolute ζ-potential values, enhanced viscoelastic properties, and a reduced creaming index. However, at 600 W, further structural modification and possible protein association may have contributed to the decline in emulsifying performance. These findings suggest that appropriate ultrasound treatment can improve the emulsifying performance of CMP under the conditions investigated, providing insights into its potential application in protein-based emulsion systems.

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Cite

BibTeXRIS
BibTeX
@article{zhou2026ultrasounddriven,
  title = {{Ultrasound-Driven Conformational Rearrangement of Coilia ectenes taihuensis Myofibrillar Protein Enhances Emulsion Stability}},
  author = {Xinhui Zhou and Zhangyan Sun and Lijun Zhu and Suting Zhuang and Xiu Wang and Changjun Zhu and Mingfeng Xu},
  journal = {Molecules},
  year = {2026},
  month = nov,
  doi = {10.3390/molecules31213966},
  url = {https://www.mdpi.com/1420-3049/31/21/3966},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Ultrasound-Driven Conformational Rearrangement of Coilia ectenes taihuensis Myofibrillar Protein Enhances Emulsion Stability
AU  - Xinhui Zhou
AU  - Zhangyan Sun
AU  - Lijun Zhu
AU  - Suting Zhuang
AU  - Xiu Wang
AU  - Changjun Zhu
AU  - Mingfeng Xu
PY  - 2026
DA  - 2026/11/03
JO  - Molecules
DO  - 10.3390/molecules31213966
UR  - https://www.mdpi.com/1420-3049/31/21/3966
AB  - Myofibrillar protein (MP) from Coilia ectenes taihuensis (CMP) has potential as a natural emulsifier; however, its relatively compact native structure may restrict its functional performance. This study evaluated the effects of ultrasound treatment (0–600 W) on CMP conformational characteristics and the stability of CMP-based emulsions. Ultrasound-induced power-dependent structural and oxidative modifications in CMP, as evidenced by increased carbonyl content, decreased sulfhydryl content, secondary structure rearrangement, and altered surface hydrophobicity. Under the conditions tested, CMP treated at 450 W exhibited the highest surface hydrophobicity and enhanced solubility, which were associated with improved emulsifying properties. The emulsifying activity index increased from 39.93 m2/g to 82.17 m2/g, accompanied by reduced droplet size, higher absolute ζ-potential values, enhanced viscoelastic properties, and a reduced creaming index. However, at 600 W, further structural modification and possible protein association may have contributed to the decline in emulsifying performance. These findings suggest that appropriate ultrasound treatment can improve the emulsifying performance of CMP under the conditions investigated, providing insights into its potential application in protein-based emulsion systems.
SN  - 1420-3049
ER  -