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Fabrication of pea protein gels with modulated rheological properties using high pressure processing
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High-pressure processing can apply non-thermal pressure to unfold protein structure and facilitate molecular interactions, yielding gels with controlled texture without thermal degradation.
“High‐pressure processing can apply the non‐thermal pressure to unfold protein structure and facilitate molecular interactions, yielding gels with controlled texture without thermal degradation (S. Zhang, Han et al. 2023).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as S. Zhang, Han et al. 2023
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“…reversible [42] pH-induced Good elasticity and high water holding capacity [43] freezing and thawing method Minimum dehydration contraction level of 15% [43] pH-induced Soybean isolation protein (SPI) implies a highly purified and concentrated version of soy protein obtained from soybeans.”
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“Furthermore, the effect of high-pressure processing (HPP) on the protein conformation analysis, the microstructure, strength of the pea protein gel, and gel rheology and dissolution were studied based on the high-pressure level, treatment time, protein concentration, and pH [109].”
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Self-citationGelation properties of three common pulse proteins: Lentil, faba bean and chickpea
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“Pea protein gels have been studied previously by Zhang et al. 38 They saw gel formation ( G 0 4 G 00 ) with 10–15% w/v protein after high pressure homogenization at 300 and 600 MPa.”
InfluentialHigh-pressure homogenization improves functional properties of pea protein isolates
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“However, such a clear effect was not observed for inulin–protein gels induced by a pressure of 300 MPa.”
BackgroundModification of pea protein gels: Extending applications in future food industry.
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InfluentialStructural and techno-functional modifications of pea protein fractions by non-thermal technologies
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“HPP has an impact on the PP gel microstructure, as HPP directly induces the formation of PP gels (Zhang, Han, and Chen 2023).”
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Alteration of proteins upon high-pressure processing treatment
Yıldız, G., & Yıldız, G. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-28973-6.00005-5
High-pressure treatment for modification of plant-based protein
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Shukla, V., Yang, Y., & Padilla‐Zakour, O. I. (2025) · Gels · doi:10.3390/gels11120972
“HPP has been shown to enact these functional and structural changes in pulse protein solutions, leading to gelled products [11,12].”
Zhang, R., Wilms, P., & van der Goot, A. J. (2026) · Applied Food Research · doi:10.1016/j.afres.2026.102342
Zhou, Y., Pan, F., Chen, H., Fang, X., Peng, W., Li, X., & Tian, W. (2026) · Food Research International · doi:10.1016/j.foodres.2026.120797
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Self-citationXu, J., Hashim, S. B. H., Xu, H., Zhang, A., Ren, J., Zou, X., Sun, Q., & Shi, J. (2026) · Gels · doi:10.3390/gels12100879
“Pressure shifts volume-dependent equilibria, promoting oligomer dissociation, hydration changes, partial unfolding, and pressure-history-dependent reassembly while leaving most covalent bonds comparatively resistant [40,90].”
Metadata
- Authors
- Zhang, S., Han, J., & Chen, L.
- Affiliations
- University of Alberta (CA)
- Corresponding author
- Chen, Lingyun
- Venue
- Food Hydrocolloids
- Publisher
- Elsevier BV
- Published
- 2023-11
- Volume
- 144
- Pages
- 109002
- ISSN
- 0268-005X (ISSN-L)
- OpenAlex
- W4381614394
- Cited by
- 53
- References
- 47
- Citations by year
- 2026: 14 · 2025: 26 · 2024: 11 · 2023: 2
- FWCI
- 7.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Food Hydrocolloids (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Microbial Inactivation Methods
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
- Keywords
- pea protein, high pressure processing, protein gels, gel rheology, gel microstructure, pH effect, protein conformation, hydrophobic interactions, hydrogen bonding, water holding capacity, freeze-thaw stability, syneresis, non-thermal food processing
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