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Structure, gelation mechanism of plant proteins versus dairy proteins and evolving modification strategies
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Soy protein isolates: A review of their composition, aggregation, and gelation.
Zheng, L., Regenstein, J. M., Zhou, L., & Wang, Z. (2022) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12925 · Cited by 266
Strong and elastic pea protein hydrogels formed through pH-shifting method
Zhu, P., Huang, W., Guo, X., & Chen, L. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.106705 · Cited by 130
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Protein–Carbohydrate Interactions in Food Matrices and Their Effects on Food Quality
Ramzan, M., Wang, A., Wu, L.-G., & Haseeb, M. A. (2026) · Foods · doi:10.3390/foods15122213 · Cited by 6
“However, to obtain this reaction, it is necessary that reaction conditions like temperature, pH, ionic strength and reaction time are modified [61].”
Sharma, S., Yadav, K., Ngasotter, S., Gulati, R., Bhalavey, P., Yadav, R., Gurawa, K., Hooda, D., Patel, N., & Majoka, S. (2026) · Food Research International · doi:10.1016/j.foodres.2025.118242 · Cited by 6
Effect of NaCl on gel mechanical behavior of bovine serum albumin–soy protein blends
Liang, G.-J., Chen, W.-P., Chen, Q.-M., Wang, Z.-J., He, Z.-Y., Zeng, M.-M., Goff, H. D., & Chen, J. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.107162 · Cited by 6
Karakuş, M. Ş. (2025) · Polymers · doi:10.3390/polym17141938 · Cited by 6
“In essence, improved gelation imparts advantages to the films, such as enhanced mechanical properties and superior gas barrier capabilities [16,17].”
Lian, Y., Liu, M., Eid, M., Wang, L.-F., & Xiong, W.-F. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111225 · Cited by 6
Yuan, H.-B., Tang, C., Chen, C., Yu, H.-Y., & Tian, H.-X. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112610 · Cited by 6
An oriented freezing strategy for fabricating fibrous structures of plant-based chicken analog
Lin, Y., Peng, Y., Shen, L., Han, Q., Li, Q., Liao, X.-J., & Zhao, J. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.112036 · Cited by 6
Zhu, B., Feng, X., Li, Y., & Qi, B. (2026) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.70421 · Cited by 5
Mueed, A., Ahmad, A., Ghazali, M. H., Zhang, M., Butt, A., Saleem, F., & You, L.-J. (2026) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2026.105713 · Cited by 5
He, K., Yao, G., Wu, R., Zhang, S., Zhang, D., Min, J., Cheng, F., Bao, Y., Zhao, S., & Wu, J. (2025) · Food Research International · doi:10.1016/j.foodres.2025.117680 · Cited by 4
Zhang, J., Li, X., Xiong, W.-F., Yao, Y., Mo, C., Cao, W., & Wang, L.-F. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.146780 · Cited by 5
Tajmousavilangerudi, A., Viretto, C., Anzelini, N., Stringari, A., Prati, A., Larcher, M., Gobbetti, M., Cagno, R. D., & Tlais, A. Z. A. (2025) · Current Research in Food Science · doi:10.1016/j.crfs.2025.101194 · Cited by 5
“This effect can be attributed to the presence of polysaccharides and plant proteins, which form more rigid gel networks (Tang et al., 2024).”
Miyashita, N. M. R., Hudson, E., Rezende, J. D. P., Vidigal, M., & Pires, A. C. D. S. (2025) · Foods · doi:10.3390/foods14081286 · Cited by 5
“Despite its advantages, US protein extraction faces challenges such as heat generation, free radical formation, and limited scalability [49].”
Transforming acid whey retentate into effective fat replacer in fat-free cream cheese
Limit, D., You, K.-M., Benson, P., Dallas, D., & Chen, D. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111718 · Cited by 5
Wang, S., Gao, Y.-X., Sun, C.-X., Li, X.-Y., Zhao, Y.-G., Cao, Y.-P., Lu, W., & Fang, Y.-P. (2025) · Food Research International · doi:10.1016/j.foodres.2025.117388 · Cited by 4
Effects of pre-heating defatted soybean slurry on flavor and functionality of soy protein isolate
Kai, Y., Lu, Y.-Y., Liu, Y., & Liu, S.-Q. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.107994 · Cited by 4
Ding, S.-S., Wang, Z.-C., Zhou, Y., Wang, Y.-X., Du, Y., Hu, J., & Wu, D. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119888 · Cited by 3
Tian, J., Wang, C., Hu, X., Shan, M., Khan, M. U., & Chen, Z. (2026) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2026.105845 · Cited by 3
Gundogan, R., Akkuzu, N., Karaça, A. C., & Capanoglu, E. (2026) · Critical reviews in food science and nutrition · doi:10.1080/10408398.2026.2647091 · Cited by 3
“However, the larger molecular size and compact globular arrangement of plant proteins make them susceptible to aggregation during heat treatment, which results in gels with low strength (Tang et al. 2024).”
Rheological and Bioactive Profile of Gelatin—Hemp Protein Hydrogels
Juchniewicz, S., & Harasym, J. (2026) · Molecules · doi:10.3390/molecules31050885 · Cited by 3
Zhou, X.-Q., Zhang, Q., Zhang, Y., Lan, T., Wang, J., & Sui, X.-N. (2026) · Food Research International · doi:10.1016/j.foodres.2026.118507 · Cited by 3
Suspension Fertilizers Based on Waste Organic Matter from Peanut Oil Extraction By-Products
Xiang, S., Li, B., & Lyu, Y. (2025) · Agronomy · doi:10.3390/agronomy15081885 · Cited by 3
Hosseini, A. F., Iqbal, A., & Rizvi, S. S. H. (2025) · Food and Bioprocess Technology · doi:10.1007/s11947-025-03964-w · Cited by 3
“6 and 7) facilitate stronger protein–protein interactions and network formation at lower concentrations (Cen et al., 2022; Sheikh et al., 2023a, b; Tang et al., 2024).”
Marinacci, A., Peyrano, F., Scilingo, A., Piermaria, J., & Speroni, F. (2025) · Sustainable Food Proteins · doi:10.1002/sfp2.70017 · Cited by 3
“Moreover, the forces that stabilize plant protein gels are mostly physical interactions (Tang et al. 2024).”
Ma, Y., Xiong, Y.-L. L., & Jiang, J. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.106311 · Cited by 3
Eswaran, U. G. M., Gupta, R. K., Idrishi, R., Muthrajan, M., Rajan, D., Giridharaprasad, S., Kumar, S., Pipliya, S., Ravichandran, S., & Srivastav, P. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119898 · Cited by 2
Wang, Z.-P., Huang, X.-W., Zhao, Y., & Wu, L.-Y. (2026) · Food Chemistry: X · doi:10.1016/j.fochx.2026.104554 · Cited by 2
“These cross-linking reactions lead to an increase in protein molecular weight and promote the formation of polymeric networks, thereby enhancing both structural stability and the capacity for network formation (Tang, Roos, & Miao, 2024; Wu et al., 2023).”
Tutu, C. O., Asiedu, B., Akonor, P., Acheampong, R., Obeng, R., Kortei, N., Wiafe-Kwagyan, M., Ulzen, J., Owusu-Bempah, J., & Mahama, S. (2026) · Applied Food Research · doi:10.1016/j.afres.2026.102623 · Cited by 2
Zhang, W.-Y., Lu, H.-B., Lu, Y., Sun, Y., Du, G., Zhao, Y., Sun, Y.-H., Yang, N.-Z., Bo, L., Ren, J., et al. (2026) · Foods · doi:10.3390/foods15112015 · Cited by 2
“Beyond providing all essential amino acids for human growth and maintenance, milk protein exhibits a range of bioactivities, such as immunomodulatory, antioxidant, and lowering effects [2,3].”
Incorporating plant proteins into cheese: opportunities and challenges (a review)
Sarker, M., Pillidge, C., Afshari, R., Chandrapala, J., & Gill, H. (2026) · Critical reviews in food science and nutrition · doi:10.1080/10408398.2026.2645263 · Cited by 2
“While plant-based proteins offer promising alternatives to animal proteins (Tang et al. 2024), they often lack cohesive and viscoelastic properties (Salgado et al. 2023; Sözeri Atik & Huppertz, 2025).”
Niu, C., Zhang, H., Tan, Y.-T., Bao, Z., & Li, D.-M. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112718 · Cited by 2
Effect of ultrasound treatment on the properties of lotus seed protein gel
Deng, X.-Y., Hao, M., Yang, J., Sun, G., Li, Y., Wang, C.-Y., Liang, Y., & Mo, H. (2025) · The Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.70119 · Cited by 2
Kanwal, N., Zhang, M., Law, C., Khan, S., & Huang, J. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.107017 · Cited by 2
Ojesanmi, A. A., & Amonsou, E. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.106854 · Cited by 2
Design of protein-rich structured liquids for management of dysphagia
Akanno, A., Girard, A. L., & Härtel, R. (2026) · Current Opinion in Food Science · doi:10.1016/j.cofs.2026.101458 · Cited by 1
Kong, X.-X., Tang, W.-T., Li, M., Sun, Q., & Pu, C.-F. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119657 · Cited by 1
Li, Z., Dai, T., Lu, Y., Geng, Q., Shuai, X., Chen, Z., Deng, L., Dong, H., & Chen, J. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119120
Siripan, T., Li, H., & Siriamornpun, S. (2026) · Foods · doi:10.3390/foods15071169 · Cited by 1
“Rice-based samples exhibited slightly higher tan δ values than soy-containing systems, indicating a relatively greater viscous contribution; however, all formulations maintained stable gel-like behavior across the tested frequency range [57,58].”
Zhu, Y.-B., Zhao, B., Li, A., Luo, J., Li, J.-N., Sheng, J., Tian, Y., & Li, X.-F. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112625 · Cited by 1
Triaxial shear behaviors of biopolymer-stabilized clayey soil under varying moisture and confinement
Cheng, Z.-B., & Geng, X. (2026) · Journal of Rock Mechanics and Geotechnical Engineering · doi:10.1016/j.jrmge.2025.12.043 · Cited by 1
Cold-set gelation of whey proteins: Principles, mechanisms, and food applications.
Cortez-Trejo, M. C., Román-Doval, R., Abadía-García, L., Cruz‐Aldaco, K., & Amaya-Llano, S. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112695 · Cited by 1
Jia, K., Liu, J., Yu, S., Wu, J., Huang, Y., Peng, Y., Wang, W., Zhao, Y., Jin, Y., Sun, P., et al. (2026) · Frontiers in Nutrition · doi:10.3389/fnut.2026.1754468 · Cited by 1
“Similar protein–bioactive compound interactions have been reported to improve the rheological and physical properties of fermented dairy products (33, 34).”
Libberecht, S., Ristevska, M., Gibis, M., & Loeffler, M. (2025) · Foods · doi:10.3390/foods15010048 · Cited by 1
“The differences in gelation properties between plant-based and animal-based proteins are the subject of ongoing research, and the key factors influencing gelation have been comprehensively discussed in recent reviews [14,15].”
Li, J., Wang, W., Yuan, X., Chen, F., Hu, X.-S., Ma, L.-J., & Ji, J.-F. (2025) · Food Research International · doi:10.1016/j.foodres.2025.117825 · Cited by 1
Dong, X., Wang, J., Wu, P., Selomulya, C., Wang, Y., & Chen, X.-D. (2025) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2025.112859 · Cited by 1
Colloidal aspects of cheese and protein-based cheese analogues
Ahrné, L., & Leser, M. (2025) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2025.101942 · Cited by 1
Zhao, X., Zhang, H.-J., Wang, K.-L., Li, J.-P., Tian, B., & Wang, S. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113287 · Cited by 1
Zhao, X., Wang, K.-L., Han, L.-Y., Li, J.-P., Tian, B., & Han, X. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.151532
Xiong, J.-J., Jiang, D.-M., Feng, G.-M., Liu, Y., Li, R., Cui, Y.-Q., Cao, W.-X., Chang, Z.-Y., Niu, Y.-N., Zou, C.-J., et al. (2026) · Food Research International · doi:10.1016/j.foodres.2026.121120
Ying, D.-C., Li, J.-H., Hu, Z.-C., Qian, T.-Y., Bao, Y.-L., Yu, Z.-Y., & Yang, Z. (2026) · Foods · doi:10.3390/foods15213875
Stępień, A., Koronowicz, A., & Jamróz, E. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.151480
Chu, Y.-F., Chen, W., Hang, J.-Y., Hu, J.-N., & Chen, L. (2026) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2026.105984
Plant-Based Fat Substitutes: From Structural Design to Application-Specific Performance
Men, S.-D., Xu, Y.-H., Liu, J.-W., Wang, Y., Yang, H., Zeng, X.-B., & Yu, H.-S. (2026) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2026.106123
Zahir, A., Akbar, U., Mondol, M. S. A., & Hakeem, K. R. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113552
Wang, Y., Yan, M., Pingli, X., Jinyin, X., Fang, D., Wang, X., Zhang, S., Zhang, Y., Wei, T., & Guo, X. (2026) · Journal of Systematics and Evolution · doi:10.1111/jse.70108
“These attributes position C. gladiata as a promising candidate for ensuring global food security and as a high ‐ value cash crop (Goyal et al., 2024; Malila et al., 2024; Tang et al., 2024b).”
InfluentialSakadani, E., Kandylis, P., & Dimitrellou, D. (2026) · Food and Bioprocess Technology · doi:10.1007/s11947-026-04547-z
“…dependent on protein source, dairy-to-plant protein ratio, processing conditions, and environmental factors, resulting in qualitative rather than universally applicable quantitative relationships between protein secondary structure and gel network properties (Rout et al., 2024; Tang et al., 2024).”
Qi, W., Zhang, Y., Li, S., Jiang, L., Sun, Y., & Sui, X. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.150875
Soy Protein-Based Hydrogels: Recent Advances in Molecular Design and Functional Applications
Li, Z.-J., Wang, L.-H., Wang, L.-Y., Yin, M., Zhang, L., Wang, X., Guo, L.-M., Chen, X.-M., & Li, C. (2026) · Gels · doi:10.3390/gels12090761
Metadata
- Authors
- Tang, Q., Roos, Y. H., & Miao, S.
- Affiliations
- Teagasc - The Irish Agriculture and Food Development Authority (IE)
- University College Cork (IE)
- Corresponding author
- Miao, Song
- Venue
- Trends in Food Science & Technology
- Publisher
- Elsevier BV
- Published
- 2024-05
- Volume
- 147
- Pages
- 104464
- ISSN
- 0924-2244 (ISSN-L)
- OpenAlex
- W4393131788
- Cited by
- 137
- References
- 0
- Citations by year
- 2026: 65 · 2025: 61 · 2024: 11
- FWCI
- 29.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Trends in Food Science & Technology (publishedVersion)
- Funders
- TEAGASC
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
- Keywords
- plant proteins, milk protein, protein gelation, protein structure, heat-induced gels, protein denaturation, casein micelles, protein modification, chemical modification, physical modification, biological modification, complex coacervation, enzymatic hydrolysis, transglutaminase
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