Effect of polyphenols on the rheology, microstructure and in vitro digestion of pea protein gels at various pH
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Polyphenols such as gallic acid and green tea polyphenol reduced gel digestibility.
“polyphenols such as gallic acid (S. Yan, Wang, et al. 2024) and green tea polyphenol (D. Chen, Stone, et al. 2024) reduced gel digestibility.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as D. Chen, Stone, et al. 2024
Cites
Guo, Y., Bao, Y.-H., Sun, K.-F., Chang, C., & Liu, W.-F. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2020.106293 · Cited by 223 · see citing works
Tombs, M. P. (1974) · Faraday Discussions of the Chemical Society · doi:10.1039/dc9745700158 · Cited by 216 · see citing works
Influence of pH and ionic strength on the thermal gelation behaviour of pea protein
Tanger, C., Müller, M., Andlinger, D., & Kulozik, U. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.106903 · Cited by 180 · see citing works
Pepsin diffusivity in whey protein gels and its effect on gastric digestion
Luo, Q., Borst, J. W., Westphal, A. H., Boom, R. M., & Janssen, A. E. M. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.11.046 · Cited by 123 · see citing works
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Drozdov, A., & Christiansen, J. (2024) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2024.112150 · Cited by 23 · see citing works
Modulating the gelling behavior of pea proteins through glutaminase-induced deamidation
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Self-citationAn, Y., Guo, R.-Q., Gao, Y., Zhu, Y., Huang, Y.-Y., Liu, L.-L., & Zhu, X.-Q. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.138252 · Cited by 18 · see citing works
Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion
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Chen, X.-J., Nie, K., Huang, X., Li, H., Wu, Y., Huang, Y., & Chen, X.-Q. (2024) · Food Chemistry: X · doi:10.1016/j.fochx.2024.102028 · Cited by 17
Wang, Y., Dong, X.-Q., Zhang, Y.-G., Zhang, Y.-M., Wang, W., Liu, Y., Zhou, S., Luo, J., Liu, J., Wu, Y.-S., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143735 · Cited by 14
Chang, J.-X., Zeng, Y., Tao, H.-B., Hu, D., Zhao, W., Wang, S., & Cao, C.-J. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.145662 · Cited by 13
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
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Liu, Q., Wang, T., Nian, B., Ma, F., Zhao, S.-Q., Vásquez, A., Guo, L.-P., Ding, C., & Davari, M. D. (2025) · Biotechnology Advances · doi:10.1016/j.biotechadv.2026.108803 · Cited by 10 · see citing works
So, H., Jun, S., Wang, Y., Du, Z., & Yang, Z. (2026) · Colloids and Surfaces A: Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2025.139273 · Cited by 9 · see citing works
Yang, Z. (2026) · Food Biomacromolecules · doi:10.1002/fob2.70048 · Cited by 9 · see citing works
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He, Y., Wang, Y., Li, Y., Guo, F., Dong, L.-L., Zhu, Z., Min, C., & Cao, Y. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.140568 · Cited by 6 · see citing works
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“The process of non-covalent binding is reversible, and the process of covalent binding is irreversible (Chen et al., 2024).”
Digestion of protein-phenolic complex: interactions, matrix effects and digestibility
Günal-Köroğlu, D., Ozkan, G., Kamiloğlu, S., Tomaş, M., Ozdal, T., & Çapanoğlu, E. (2026) · Critical reviews in food science and nutrition · doi:10.1080/10408398.2026.2687770 · Cited by 4 · see citing works
“Conversely, phenolic acid-induced conformational changes, such as protein unfolding and exposure of hydrophobic regions, can enhance enzyme accessibility and promote proteolysis (Chen et al. 2024; Shi et al. 2024).”
InfluentialPanza, O., Alfieri, M., Nobile, D., Mugnaini, G., Conte, A., Panzella, L., & Bonini, M. (2025) · LWT · doi:10.1016/j.lwt.2025.118029 · Cited by 4
Lin, Q., Liang, W., Zhao, W.-Q., Zeng, J., Gao, H.-Y., & Li, W. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.145274 · Cited by 4
Jiang, C., Liu, F., Ma, Z., Wang, J., Zhang, H., Zhang, T.-H., & Wang, C.-N. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112822 · Cited by 3
Shen, L.-P., Wei, S., Han, Z.-Y., Pan, Y.-M., Yin, Y., Shao, J.-H., & Liu, S.-C. (2026) · Food Research International · doi:10.1016/j.foodres.2026.118935 · Cited by 3
Ajayi, F. F., You, K.-M., Maqsood, S., & Chen, D. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112549 · Cited by 3 · see citing works
Self-citationRegulation of Tea Polyphenols on the Gel Properties of Soy Protein and the Action Mechanism.
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Li, Z., Huang, X.-H., Hu, Y.-M., Gafurov, K., Zhang, J.-C., Wang, Q., & Guo, Q. (2026) · Food Research International · doi:10.1016/j.foodres.2026.119700 · Cited by 2
Zha, Z., Yu, J., Wang, X.-Z., Li, D.-L., Zhang, M., Zeng, X.-M., Wang, X., Wang, X.-M., Zhao, D., & Li, C.-B. (2026) · Food Research International · doi:10.1016/j.foodres.2026.118759 · Cited by 2
Li, J.-L., Shen, J.-X., Shen, W.-Y., Jin, W.-P., Guo, C., Xiong, S.-B., & Hu, Y. (2026) · Food Chemistry: X · doi:10.1016/j.fochx.2026.103742 · Cited by 2 · see citing works
“EGCG (in the form of green tea polyphenols, GTP) reduced the digestibility of pea protein by approximately 7.4% under conditions of pH 8.5 and 1% GTP (Chen et al., 2024).”
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“Previous studies on plant-extract-enriched emulsions have also shown that polyphenols and low-molecular-weight sugars increase tan δ by reducing interparticle cohesion, resulting in softer, less sticky formulations [43,44].”
Aggregated-state remodeling of quinoa protein gels by thermal pretreatment and transglutaminase.
Quan, Z.-Y., Ji, T., Liu, J., Zeng, D.-P., Zhang, X.-N., Chen, Y., Qian, J.-Y., & Zhang, L. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.149559 · Cited by 1 · see citing works
Wang, X., Meng, D.-K., Han, S., Zhang, H., Li, H.-Y., Xu, Y.-H., Xu, L.-N., Xia, N., Si, P.-Y., Ghamry, M., et al. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.149008 · Cited by 1 · see citing works
Su, K.-Y., Liu, J., Yang, L., Li, B.-Z., Guo, Z.-R., Wang, Y.-J., Wang, J.-L., Zhang, W.-T., & Shi, S. (2026) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6c09006
Zhang, L., Sun, Y.-N., Liang, Y.-Q., Wang, Y., Li, J.-M., & Zang, J. (2026) · ACS Food Science & Technology · doi:10.1021/acsfoodscitech.6c00078
Cocean, A.-M., Teleky, B.-E., Martău, G., Varvara, R.-A., Ranga, F., Medeleanu, M., Tokos, K., & Vodnar, D. (2026) · Journal of Food Measurement & Characterization · doi:10.1007/s11694-026-04877-8
“…proteins and polyphenols also play an important role: SB flavonoids, such as quercetin and isor - hamnetin, form non-covalent complexes with proteins in peanut butter and oats, thereby increasing rigidity and water retention capacity through both hydrogen bonding and hydrophobic interactions [66].”
Chang, Y.-Z., Hong, J.-H., Wang, H.-B., Wen, Y.-T., Fu, W.-Y., Fang, G.-Y., Wu, C.-L., Wu, F.-H., Liu, X.-Q., & He, Z.-P. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.151038
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Yang, J., Zhang, L.-Q., Kuang, Y., Wu, S., Huang, H., & Song, J.-J. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.151093
Pati, B., Priyadarshini, M., Mehta, N., Patel, A. B., Gaurav, K., & Anand, S. (2026) · Gels · doi:10.3390/gels12090776
“Likewise, Chen et al. [64] reported that increasing concentrations of green tea polyphenols in protein gels progressively reduced the onset and denaturation temperatures, together with the denaturation enthalpy ( ∆ H decreased from 7.13 to 6.45 J/g at pH 5), which is consistent with the reduced ∆ H…”
InfluentialLe, T.-H.-A. (2026) · Food and Bioprocess Technology · doi:10.1007/s11947-026-04511-x
“Adding phenolics before heating may allow them to participate in unfolding and aggregation, whereas adding them after protein gelation or emulsification may mainly affect surface binding, antioxidant partitioning, or sensory perception (Chen et al., 2024).”
InfluentialFahrullah, F., Basriani, B., Anita, C., Febryanti, F., & Fitriyani, F. (2025) · Jurnal Pangan dan Agroindustri · doi:10.21776/ub.jpa.2025.013.01.4
“Interaksi ini menghambat pembentukan jaringan protein yang diperlukan untuk gelasi, sehingga memperpanjang waktu gelasi (Chen et al., 2024).”
Wei, L., Husseini, S., Constantin, C., You, K.-M., Ilavsky, J., Jones, O., Jiménez-Flores, R., Liceaga, A., & Chen, D. (n.d.) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113315
Self-citation
- Authors
- Chen, D., Stone, S., Ilavsky, J., & Campanella, O.
- Affiliations
- Purdue University West Lafayette (US)
- The Ohio State University (US)
- Corresponding author
- Chen, Da
- Campanella, Osvaldo
- Venue
- Food Hydrocolloids
- Publisher
- Elsevier BV
- Published
- 2024-06
- Volume
- 151
- Pages
- 109827
- ISSN
- 0268-005X (ISSN-L)
- OpenAlex
- W4391301177
- Cited by
- 51
- References
- 0
- Citations by year
- 2026: 23 · 2025: 19 · 2024: 9
- FWCI
- 10.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (am, 245 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Food Hydrocolloids (acceptedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- Jiangsu Provincial Key Laboratory of Environmental Engineering, Jiangsu Provincial Academy of Environmental Science
- Argonne National Laboratory (DE-AC02-06CH11357)
- Purdue University
- Office of Science
- Ohio State University
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Keywords
- pea protein, green tea polyphenols, protein-polyphenol interactions, protein gels, gel rheology, gel microstructure, in vitro protein digestion, pH effect, storage modulus, critical strain, heat resistance, protein aggregation, radius of gyration
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