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Exposure of hydrophobic groups affected the thermal aggregation of myosin based on experimental and molecular dynamics simulation
Open accessAbstract
In this study, Beijing duck breast myosin was used to analyze the structural and functional changes during thermal treatments. The particle size and atomic force microscopy (AFM) imaging results showed that the myosin polymer formed generously at 55 °C. Meanwhile, the myosin denatured and unfolded at 50–55 °C leading to the exposure of hydrophobic groups detected by structural determinations including circular dichroism (CD), sulfhydryl content and Ca2+-ATPase activity. The increase of hydrophobic interaction was observed to promote the myosin aggregation at 55 °C, and disulfide bonds played a supplementary role in the stabilization of myosin aggregates at 80 °C. Molecular docking and dynamics simulation verified that electrostatic energy of myosin decreased on reaching 55 °C, and the hydrophobicity increased to promote the aggregation while kinetic energy increased at 80 °C. The presented study provided a potential selection of processing temperature conditions from the aggregation of protein.
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“In details, proteins contain abundant hydrophobic groups and most gelation processes involve protein unfolding exposing additional hydrophobic residues (X. Wei, Monahan, et al. 2023; Gorissen et al. 2018), which can make hydrophobic interaction a major driving force in gel network formation.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as X. Wei, Monahan, et al. 2023
Citations
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Lee, S., Jo, K., Kim, S., Han, S., & Jung, S. (2025) · Food Chemistry: X · doi:10.1016/j.fochx.2025.102886 · Cited by 24
“Wei et al. (2023) re-ported that myosin denatured at 50 ◦ C without forming large aggregates; however, at 55 ◦ C, protein cross-linking increased owing to tail helix destabilization, suggesting that 55 ◦ C is a critical threshold for myosin structural transformation.”
Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion
Dong, X., Wang, Y., Chen, X. D., & Selomulya, C. (2026) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.70424 · Cited by 17
Ding, Y.-X., Feng, R., Zhu, Z., Xu, J., & Xu, Y.-S. (2024) · Food Chemistry: X · doi:10.1016/j.fochx.2024.101448 · Cited by 16
Wang, Y.-D., Zhuang, Y., Zhang, J., Chen, Y., & Yang, H. (2024) · LWT · doi:10.1016/j.lwt.2024.115865 · Cited by 13
Zhang, Q.-Q., Yuan, L., Kong, Y., Xiong, Z., Bao, Y.-L., & Gao, R.-C. (2025) · Food Chemistry: X · doi:10.1016/j.fochx.2025.102756 · Cited by 9
“This may be attributed to thermal aggregation-induced spatial site-barrier effects that directly impact enzyme accessibility(Wei et al., 2023).”
Metadata
- Authors
- Wei, X., Monahan, F., Zhang, C., Wang, Z., & Zhang, D.
- Affiliations
- University College Dublin (IE)
- Institute of Food Science and Technology (CN)
- Corresponding author
- Wang, Zhenyu
- Zhang, Dequan
- Venue
- LWT
- Publisher
- Elsevier BV
- Published
- 2023-09
- Volume
- 187
- Pages
- 115315
- ISSN
- 0023-6438 (ISSN-L)
- OpenAlex
- W4386815654
- Cited by
- 21
- References
- 41
- Citations by year
- 2026: 11 · 2025: 5 · 2024: 5
- FWCI
- 3.67
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- LWT (publishedVersion, cc-by-nc-nd)
- Funders
- National Key Research and Development Program of China (2019YFC1606200, CAAS-ASTIP-2018-IAPPST-2)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- myosin, thermal aggregation, hydrophobic groups, protein denaturation, disulfide bonds, hydrophobic interactions, protein unfolding, electrostatic energy, Ca2+-ATPase activity
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- Wei, X., Monahan, F., Zhang, C., Wang, Z., & Zhang, D. (2023). Exposure of hydrophobic groups affected the thermal aggregation of myosin based on experimental and molecular dynamics simulation. LWT. https://doi.org/10.1016/j.lwt.2023.115315
