Modifying yellowfin tuna myofibrillar proteins under ultra-high pressure auxiliary heat treatment: Impact on the conformation, gel properties and digestive characteristics
Abstract
This study investigated the changes in physicochemical and functional properties of yellowfin tuna myofibrillar protein (MP) under various ultra-high pressure (UHP) auxiliary heat methods. The UHP-assisted heat treatment induced a rearrangement of the MP secondary structure, facilitating the formation of MP gel networks and resulting in higher storage modulus (G') values. Microstructure results revealed that MP gel produced with UHP auxiliary heat exhibited a more rigid network. As pressure increased, the regular aggregation of protein molecules enhanced the stability and water-binding capacity within the gel network, particularly under the two-stage UHP auxiliary heat (TUH) condition at 300 MPa. MP gel prepared under this condition exhibited a 1.95-fold increase in gel strength compared to the control group and the lowest creep strain. Furthermore, in vitro simulated digestion results indicated that TUH method significantly improved the digestive properties of MP gel, suggesting potential for the development of easily digestible MP-based gel foods.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
This structural rearrangement from UHP led to higher mechanical strength and protein digestibility, attributed to UHP-induced exposure of additional enzymatic cleavage sites on protein molecules.
“This structural rearrangement led to higher mechanical strength and protein digestibility, attributed to UHP‐induced exposure of additional enzymatic cleavage sites on protein molecules”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Z. Tan, Yang, et al. 2025
UHP treatment can modulate the secondary structure of proteins, promoting molecular chain unfolding and ordered protein aggregation.
“UHP treatment can modulate the secondary structure of proteins, promoting molecular chain unfolding and ordered protein aggregation.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Z. Tan, Yang, et al. 2025
Cites
β-Lactoglobulin and WPI aggregates: Formation, structure and applications
Nicolaï, T., Britten, M., & Schmitt, C. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.02.006 · Cited by 575 · see citing works
Zhang, Z., Yang, Y., Zhou, P., Zhang, X., & Wang, J. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.09.040 · Cited by 456 · see citing works
Protein Oxidation in Muscle Foods: A Comprehensive Review
Domínguez, R., Pateiro, M., Munekata, P. E. S., Zhang, W., Garcia‐Oliveira, P., Carpena, M., Prieto, M. A., Bohrer, B. M., & Lorenzo, J. M. (2021) · Antioxidants · doi:10.3390/antiox11010060 · Cited by 386 · see citing works
Liu, K., & Hsieh, F. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf073343q · Cited by 363 · see citing works
Wang, J., Xia, N., Yang, X., Yin, S., Qi, J., He, X., Yuan, D., & Wang, L. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf205128v · Cited by 328 · see citing works
Self-citationXu, X.-L., Han, M., Fei, Y., & Zhou, G. (2010) · Meat Science · doi:10.1016/j.meatsci.2010.10.001 · Cited by 244 · see citing works
Cooking‐Induced Protein Modifications in Meat
Yu, T., Morton, J. D., Clerens, S., & Dyer, J. M. (2016) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12243 · Cited by 242 · see citing works
Straadt, I. K., Rasmussen, M., Andersen, H. J., & Bertram, H. C. (2006) · Meat Science · doi:10.1016/j.meatsci.2006.09.019 · Cited by 223 · see citing works
Wei, Y., Sun, C., Dai, L., Zhan, X., & Gao, Y. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.02.042 · Cited by 212 · see citing works
Flow and Thixotropic Parameters for Rheological Characterization of Hydrogels
Ghica, M. V., Hîrjău, M., Lupuleasa, D., & Dinu‐Pîrvu, C. (2016) · Molecules · doi:10.3390/molecules21060786 · Cited by 179 · see citing works
Chen, X., Xu, X., Liu, D., Zhou, G., Han, M., & Wang, P. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.10.030 · Cited by 173 · see citing works
Evaluation of protein aggregation in cooked meat
Promeyrat, A., Gatellier, P., Lebret, B., Kajak‐Siemaszko, K., Aubry, L., & Santé-Lhoutellier, V. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2009.12.057 · Cited by 145 · see citing works
Lu, H., Zhang, L., Li, Q., & Luo, Y. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.11.143 · Cited by 133 · see citing works
Li, D., Tan, Z., Liu, Z., Wu, C., Liu, H., Guo, C., & Zhou, D. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.129344 · Cited by 132 · see citing works
Self-citationHuang, J., Bakry, A. M., Zeng, S., Xiong, S., Yin, T., You, J., Fan, M., & Huang, Q. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.08.028 · Cited by 123 · see citing works
Yi, S., Li, Q., Qiao, C., Zhang, C., Wang, W., Xu, Y., Mi, H., Li, X., & Li, J. (2020) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2020.105924 · Cited by 123 · see citing works
The Behavior of the Hydrophobic Effect under Pressure and Protein Denaturation
Grigera, J. R., & McCarthy, A. N. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.12.4298 · Cited by 115 · see citing works
The effect of the pH on thermal aggregation and gelation of soy proteins
Chen, N., Zhao, M., Niepceron, F., Nicolaï, T., & Chassenieux, C. (2016) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.12.006 · Cited by 110 · see citing works
Wu, D., Tu, M., Wang, Z.-Y., Wu, C., Yu, C.-P., Battino, M., El-Seedi, H., & Du, M. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.107491 · Cited by 101 · see citing works
Du, X., Chang, P., Tian, J., Kong, B., Sun, F., & Xia, X. (2020) · LWT · doi:10.1016/j.lwt.2020.109140 · Cited by 101 · see citing works
Lefèvre, F., Fauconneau, B., Thompson, J. W., & GILL, T. A. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf063045d · Cited by 100 · see citing works
Rheological and structural characterization of whey protein gelation induced by enzymatic hydrolysis
Tarhan, Ö., Spotti, M. J., Schaffter, S., Corvalán, C. M., & Campanella, O. H. (2016) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.04.042 · Cited by 99 · see citing works
Fan, H., Zhang, M., Liu, Z., & Ye, Y. (2019) · LWT · doi:10.1016/j.lwt.2019.109004 · Cited by 92 · see citing works
Self-citationTan, Z., Yang, X., Wang, Z.-M., Chen, Z., Pan, J., Sun, Q., & Dong, X. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.138538 · Cited by 79 · see citing works
Self-citationEstévez, M., Ventanas, S., & Cava, R. (2005) · Food Chemistry · doi:10.1016/j.foodchem.2005.09.009 · Cited by 72 · see citing works
Wang, J., Li, Z., Zheng, B., Zhang, Y., & Guo, Z. (2018) · LWT · doi:10.1016/j.lwt.2018.10.053 · Cited by 70 · see citing works
Zhang, T., Wang, J., Feng, J., Liu, Y., Suo, R., Ma, Q., & Sun, J. (2022) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2022.106218 · Cited by 66 · see citing works
Li, D., Li, N., Wang, Y., Zhang, K., Tan, Z., Liu, H., Liu, X., Wu, Q., & Zhou, D. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109595 · Cited by 65 · see citing works
Self-citationHsu, K., Hwang, J., Yu, C.-C., & Jao, C. (2006) · Food Chemistry · doi:10.1016/j.foodchem.2006.09.001 · Cited by 58 · see citing works
Combination of high pressure and heat on the gelation of chicken myofibrillar proteins
Zheng, H., Han, M., Bai, Y., Xu, X., & Zhou, G. (2018) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2018.10.014 · Cited by 58 · see citing works
Xie, Y., Yang, F. Y., Zhao, K., Zhang, W., Liu, Q., & Yuan, Y. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c05645 · Cited by 52 · see citing works
Chen, X., Chen, K., Cheng, H., & Liang, L. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c05840 · Cited by 50 · see citing works
Song, G., Chen, K., Wang, H., Zhang, M., Yu, X., Wang, J., & Shen, Q. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.126504 · Cited by 50 · see citing works
Molecular spectroscopy to assess protein structures within cereal systems
Sadat, A., Corradini, M. G., & Joye, I. J. (2019) · Current Opinion in Food Science · doi:10.1016/j.cofs.2019.02.001 · Cited by 44 · see citing works
Liu, Q., Lin, Z., Chen, X., Chen, J., Wu, J., Chen, H., & Zeng, X. (2022) · LWT · doi:10.1016/j.lwt.2022.113691 · Cited by 38 · see citing works
Chen, H., Zhou, A., Benjakul, S., Zou, Y., Liu, X., & Xiao, S. (2021) · LWT · doi:10.1016/j.lwt.2021.112086 · Cited by 37 · see citing works
The effect of pressure-assisted heating on the water holding capacity of chicken batters
Zheng, H., Han, M., Yang, H., Xu, X., & Zhou, G. (2017) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2017.11.011 · Cited by 37 · see citing works
Zhang, K., Tan, Z., Zhang, Q., Wu, Q., Zhao, J., Xu, W., Liu, Y., Liu, X., Zhou, D., & Li, D. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.142995 · Cited by 34 · see citing works
Self-citationNi, X., Li, M., Huang, Z., Wei, Y., Duan, C., Li, R., Fang, Y.-J., Wang, X., Xu, M., & Yu, R. (2025) · Food Chemistry X · doi:10.1016/j.fochx.2025.102243 · Cited by 32 · see citing works
Effects of High Pressure Modification on Conformation and Digestibility Properties of Oyster Protein
Wang, R., Jiang, S., Li, Y., Xu, Y., Zhang, T., Zhang, F., Xue, F., Zhao, Y., & Zeng, M. (2019) · Molecules · doi:10.3390/molecules24183273 · Cited by 32 · see citing works
Li, X., He, X., Mao, L., Gao, Y., & Yuan, F. (2019) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2019.109851 · Cited by 32 · see citing works
Nie, X., Liu, H., Yu, N., Tang, Q., Wu, C., & Meng, X. (2021) · Journal of Food Science · doi:10.1111/1750-3841.15965 · Cited by 32 · see citing works
Zhang, K., Li, N., Li, J., Wang, Y., Liu, C., Liu, Y., Li, D., Zhou, D., & Li, D. (2023) · Food Bioscience · doi:10.1016/j.fbio.2023.103402 · Cited by 31 · see citing works
Nourmohammadi, N., Campanella, O. H., & Chen, D. (2024) · Food Research International · doi:10.1016/j.foodres.2024.114474 · Cited by 28 · see citing works
Bird muscles under hydrostatic high-pressure/temperature combinations
Fernández-Martín, F. (2007) · Journal of Thermal Analysis and Calorimetry · doi:10.1007/s10973-006-7809-6 · Cited by 25 · see citing works
Liu, X., Mao, K., Sang, Y., Tian, G., Ding, Q., & Deng, W. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.873578 · Cited by 24 · see citing works
Fan, X. M., Zhang, K., Tan, Z., Xu, W., Liu, X., Zhou, D., & Li, D. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.141697 · Cited by 22 · see citing works
Self-citationAggregability and digestibility study of fruit juice fortified camel milk powder proteins
Khulal, U., Ghnimi, S., Stevanović, N., Rajković, A., & Veličković, T. Ć. (2021) · LWT · doi:10.1016/j.lwt.2021.112250 · Cited by 21 · see citing works
Global knowledge domain and prospects in tuna research: A bibliometric analysis
Xie, J., Bian, Z.-Q., Wu, Q., Tao, L., Wu, F., & Lin, T. (2021) · Aquaculture & Fisheries · doi:10.1016/j.aaf.2021.09.005 · Cited by 17 · see citing works
Lu, H., Liang, Y., Zhang, X., & Wen, G. (2022) · Foods · doi:10.3390/foods11030330 · Cited by 15 · see citing works
Tan, Z., Yang, X., Jin, Z., Lin, H. L., Li, K., Prakash, S., & Dong, X. (2024) · Food Chemistry X · doi:10.1016/j.fochx.2024.101480 · Cited by 15 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Tan, Z., Yang, X., Yu, X., Wang, Y., Liu, Z., & Dong, X. (2025) · Food Research International · doi:10.1016/j.foodres.2025.116605 · Cited by 18 · see citing works
Self-citationDesigning 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 · see citing works
Self-citationPeng, H., Yang, Q., Zhou, C., Wang, L., Pan, D., Cao, J., Sun, Y., Zhang, H., & Xia, Q. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c09120 · Cited by 15 · see citing works
You, Z., Chen, Y., Teng, W.-D., Wang, Y., Zhang, Y.-M., Cao, J.-X., & Wang, J.-P. (2025) · Foods · doi:10.3390/foods14081290 · Cited by 13 · see citing works
Fu, Z., Li, J., Ya, W., Cen, J., Xiang, H., Hu, X., Li, C., Wu, Y., Chen, S., Zhao, Y., et al. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.146391 · Cited by 12 · see citing works
Liu, Z., Chen, X., Chen, B., Qu, Y., Tang, H., Wu, R., Qiao, K., Su, Y., Pan, N., Chen, T., et al. (2025) · Foods · doi:10.3390/foods14091537 · Cited by 9 · see citing works
Self-citationYu, Y., Zhang, H., Chen, W., Li, Y., Chen, S., Zhang, T., Zhang, Q., Xu, Y., Du, X., & Xiufang, X. (2026) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2026.105530 · Cited by 9 · see citing works
Liu, Y., Shi, T., Cao, X., Wang, X., Li, M., Lu, C., Zhang, X., Tian, Y., Yuan, L., Jin, W., et al. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.144728 · Cited by 7 · see citing works
Zhang, L., Ge, Z., Zhang, L., & Wei, Z. W. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.112021 · Cited by 7 · see citing works
Liu, J., Zeng, X., Zhao, J., Chi, Y., Xiu, L., Zheng, M., & Liu, H. (2025) · Foods · doi:10.3390/foods14193342 · Cited by 5 · see citing works
Liu, R., Guo, Y., Yu, X., Liu, X., & Zhou, D. (2025) · Food Research International · doi:10.1016/j.foodres.2025.118037 · Cited by 5 · see citing works
Yang, X., Tan, Z., Ling, S., Jiang, K., & Dong, X. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.148085 · Cited by 4 · see citing works
Self-citationDong, K., Huang, X., Wu, Y., Jin, G., Guan, Y., Song, H., An, F., Li, X., Zhang, E., & Huang, Q. (2025) · Food Research International · doi:10.1016/j.foodres.2025.117946 · Cited by 3 · see citing works
Feng, J., Hu, M., Meng, Q., Sun, R., Lin, H., Guo, Y., Liu, S., Benjakul, S., & Zhang, B. (2026) · LWT · doi:10.1016/j.lwt.2026.119317 · Cited by 3 · see citing works
Screening, synthesis and anti-fatigue function verification of selenopeptides
Shi, L. S., Jia, W., Zhang, R., & Mo, H. (2025) · Food Research International · doi:10.1016/j.foodres.2025.117764 · Cited by 1 · see citing works
Cai, H., Bao, Z., Liu, X., Su, X., Tang, C., Xie, Y., & Xu, B. (2026) · Journal of Texture Studies · doi:10.1111/jtxs.70097 · Cited by 1 · see citing works
Liang, Q., Jiang, X., Zhang, Y., Li, Y., & Shi, W. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119111 · Cited by 1 · see citing works
Synergistic UHP-Heat Treatment of Yellowfin Tuna Surimi: Gel Properties, Mechanism Elucidation
Wang, Y., Tan, Z., Zheng, Y., Yang, J., Yu, X., Lu, Y., & Dong, X. (2026) · Journal of Future Foods · doi:10.1016/j.jfutfo.2026.04.014
Self-citationZheng, Y., Yang, X., Wang, Y., Lv, Z., Zhang, S., & Dong, X. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.152423
Self-citationXie, Y., Zhang, M., Yu, Q., & Liu, Y. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119762
Amiri, A., Korolev, V., Maggo, S., Singh, A., & Pratap-Singh, A. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.150146
Sensory quality of F. venenatum TB01 protein: Implications for next generation alternative proteins
Wang, Z., Wang, B., Yue, Z., Yang, W., Li, D., Li, W., & Wang, Y. (2026) · Food Research International · doi:10.1016/j.foodres.2026.120115
Zang, X., Zhou, S., Guo, X., Yang, G., Shi, K., Wang, L., Zhang, Z., & Sun, J. (2026) · Food Bioscience · doi:10.1016/j.fbio.2026.109601
Wang, Y., Wang, Y., Yu, X., Chi, X., Tu, J., & Dong, X. (2026) · Food Research International · doi:10.1016/j.foodres.2026.120232
Self-citationLi, Y., Yang, C., Zhang, X., Gao, Y., Zhou, D., & Li, D. (2026) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.70601
Li, M., Wan, J., Guan, W., Liu, B., Xu, X., Zhao, Q., & Fan, X. (2026) · Foods · doi:10.3390/foods15183259
Self-citationDai, J., Dong, Y., Wang, H., Lan, T., & Sui, X. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113452
- Authors
- Tan, Z., Yang, X., Zhao, W., Ma, J., Fan, X., Liu, Z., & Dong, X.
- Affiliations
- Dalian Polytechnic University (CN)
- Shenzhen University (CN)
- Corresponding author
- Dong, Xiuping
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2025-05
- Volume
- 475
- Pages
- 143365
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W4407316632
- Cited by
- 27
- References
- 52
- Citations by year
- 2026: 15 · 2025: 12
- FWCI
- 16.65
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Food Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Key Research and Development Program of China (2023YFD2100200)
- 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 › Biotechnology › Microbial Inactivation Methods
- Keywords
- yellowfin tuna, myofibrillar proteins, ultra-high pressure processing, protein secondary structure, gel properties, storage modulus, water holding capacity, gel strength, in vitro digestion, digestibility
- MeSH terms
- Animals, Digestion, Food Handling, Gels, Hot Temperature, Muscle Proteins, Myofibrils, Pressure, Protein Conformation, Tuna, Seafood, Fish Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review