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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
Cites
Effects of heat on meat proteins - Implications on structure and quality of meat products.
Tornberg, E. (2005) · Meat Science · doi:10.1016/j.meatsci.2004.11.021 · Cited by 1,325
Alizadeh-Pasdar, N., & Li-Chan, E. (2000) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf990393p · Cited by 599
Zhang, L., Wang, P., Yang, Z., Du, F., Li, Z., Wu, C., AiHu, F., Xu, X., & Zhou, G. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.105455 · Cited by 223
Functionality of muscle constituents in the processing of comminuted meat products.
Acton, J., Ziegler, G., Burge, D. L., & Froning, G. (1983) · Critical reviews in food science and nutrition · doi:10.1080/10408398209527360 · Cited by 211
A review of methods used for investigation of protein–phenolic compound interactions
Czubiński, J., & Dwiecki, K. (2017) · doi:10.1111/ijfs.13339 · Cited by 196
Gómez-Guillén, M., Borderías, A., & Montero, P. (1997) · LWT · doi:10.1006/fstl.1997.0239 · Cited by 190
Chu, L., Luo, L., & Fwa, T. (2019) · Construction and Building Materials · doi:10.1016/j.conbuildmat.2019.07.178 · Cited by 157
Thermal aggregation properties of whey protein glycated with various saccharides
Liu, G., & Zhong, Q. (2013) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2012.12.008 · Cited by 151
Chen, X., Chen, C.-G., Zhou, Y.-Z., Li, P.-J., Ma, F., Nishiumi, T., & Suzuki, A. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.03.018 · Cited by 150
Guo, X.-Y., Peng, Z.-Q., Zhang, Y.-Z., Liu, B., & Cui, Y.-Q. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2014.08.045 · Cited by 149
Herrero, A. M., Cambero, M. I., Ordóñez, J. A., de la Hoz, L., & Carmona, P. (2008) · Food Chemistry · doi:10.1016/j.foodchem.2007.12.003 · Cited by 145
Importance of salt and temperature in myosin polymerization during surimi gelation.
Núñez-Flores, R., Cando, D., Borderías, A., & Moreno, H. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2017.07.028 · Cited by 121
Liu, K., Zha, X.-Q., Li, Q.-M., Pan, L.-H., & Luo, J.-P. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.106807 · Cited by 112
The mechanism of formation of gels from myosin molecules
Sharp, A., & Offer, G. (1992) · doi:10.1002/jsfa.2740580112 · Cited by 108
Na, N., Wang, Z., He, F., Wang, L.-C., Han, P., Li, X., Wang, Q., & Zhang, D.-Q. (2014) · doi:10.1016/j.procbio.2014.01.017 · Cited by 103
Self-citationÁlvarez, D., Xiong, Y.-L., Castillo, M., Payne, F., & Garrido, M. (2012) · Meat Science · doi:10.1016/j.meatsci.2012.03.012 · Cited by 98
Dai, H., Chen, X.-K., Peng, L., Ma, L., Sun, Y., Li, L., Wang, Q., & Zhang, Y.-H. (2020) · doi:10.1016/j.foodhyd.2020.105869 · Cited by 96
Microwave irradiation promotes aggregation behavior of myosin through conformation changes
Cao, H.-W., Jiao, X.-D., Fan, D., Huang, J.-L., Zhao, J.-X., Yan, B.-W., Zhou, W.-G., Zhang, H., & Wang, M.-F. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.05.002 · Cited by 90
Zhang, Y., Dong, M. S., Zhang, X., Hu, Y., Han, M., Xu, X., & Zhou, G. (2020) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2020.105974 · Cited by 89
The dynamics of thermal denaturation of fish myosins
Chan, J. K., Gill, T., & Paulson, A. (1992) · doi:10.1016/0963-9969(92)90152-u · Cited by 84
Yongsawatdigul, J., & Sinsuwan, S. (2007) · doi:10.1016/j.foodhyd.2006.04.006 · Cited by 83
Gao, R.-C., Wang, Y.-M., Mu, J.-L., Tong, S., & Yuan, L. (2018) · doi:10.1016/j.foodhyd.2017.08.029 · Cited by 81
Tóth, G., Bowers, S., Truong, A. P., & Probst, G. (2007) · Current pharmaceutical design · doi:10.2174/138161207782794284 · Cited by 73
Xu, J., Chen, X., Yang, G., Niu, X.-L., Chang, F., & Lacidogna, G. (2021) · Construction and Building Materials · doi:10.1016/j.conbuildmat.2021.125389 · Cited by 63
Effect of resistant corn starch on the thermal gelling properties of chicken breast myosin
Wang, X., Li, Y.-S., Zhou, Y., Ma, F., Li, P., & Chen, C. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.06.013 · Cited by 59
Vaskoska, R., Ha, M., Ong, L., Chen, G., White, J., Gras, S., & Warner, R. (2021) · Meat Science · doi:10.1016/j.meatsci.2021.108521 · Cited by 54
Han, Z.-Y., Li, X.-X., Liu, Y., Yue, X., Wu, Z.-X., & Shao, J.-H. (2021) · doi:10.1016/j.foodhyd.2021.106825 · Cited by 52
Tang, C., Zhang, W.-G., Dai, C., Li, H.-X., Xu, X.-L., & Zhou, G.-H. (2015) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf5044713 · Cited by 50
Isolation of carp myosin rod and its structural stability
Kato, S., & Konno, K. (1993) · doi:10.2331/suisan.59.539 · Cited by 46
Liu, J., Puolanne, E., & Ertbjerg, P. (2014) · Meat Science · doi:10.1016/j.meatsci.2014.05.013 · Cited by 42
Ding, Y., Liu, R., Rong, J.-H., & Xiong, S.-B. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2013.10.123 · Cited by 38
Non-invasive lactate- and pH-monitoring in porcine meat using Raman spectroscopy and chemometrics
Nache, M., Scheier, R., Schmidt, H., & Hitzmann, B. (2015) · Chemometrics and Intelligent Laboratory Systems · doi:10.1016/j.chemolab.2015.02.002 · Cited by 36
Chaosap, C., Sitthigripong, R., Sivapirunthep, P., Pungsuk, A., Adeyemi, K., & Sazili, A. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.126677 · Cited by 26
Chen, Y., Liu, L.-G., Fu, H., Wei, C., & Jin, Q. (2014) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2014.09.142 · Cited by 21
Jia, Z.-J., Lan, X.-W., Lu, K., Meng, X., Jing, W.-J., Jia, S., Zhao, K., & Dai, Y.-N. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.135409 · Cited by 18
High-pressure effects on myosin in relation to heat gelation: A micro-perspective study
Xue, S., Qian, C., Kim, Y. H. B., Xu, X.-L., & Zhou, G.-H. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.06.014 · Cited by 17
Effect of Protein Thermal Denaturation on the Texture Profile Evolution of Beijing Roast Duck
Liu, Y.-X., Wang, Z.-Y., Zhang, D.-Q., Pan, T., Liu, H., Shen, Q.-W. W., & Hui, T. (2022) · Foods · doi:10.3390/foods11050664 · Cited by 14
Self-citationScheffler, T., Leitner, M. B., & Wright, S. A. (2018) · Journal of Animal Science · doi:10.1093/jas/sky283 · Cited by 14
Cao, L.-C., Hou, C., Hussain, Z., Zhang, D.-Q., & Wang, Z.-Y. (2020) · LWT · doi:10.1016/j.lwt.2020.109269 · Cited by 12
Self-citationToxicological analysis of roast duck flavor components.
Zhou, Y.-M., Yan, B., Zhao, S., Zhou, X.-L., & Xiao, Y. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.12.001 · Cited by 9
Research works printed but not linked: 2
- Foegeding, 1986, Effect of Heating Rate on Thermally Formed Myosin, Fibrinogen and Albumin Gels, Journal of Food Science, 51, 104, 10.1111/j.1365-2621.1986.tb10846.x · DOI
- Wei, 2020, The effect of age on the myosin thermal stability and gel quality of Beijing duck breast, Food Science of Animal Resources, 40, 588, 10.5851/kosfa.2020.e36 · DOI
Cited by
Sorted by citations
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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