Impacts of pH and heating temperature on formation mechanisms and properties of thermally induced canola protein gels
Abstract
The formation mechanisms and properties of thermally induced canola protein gels were investigated over a broad range of pHs (5–11) and processing temperatures (80–120 °C) involving two canola protein fractions, CP1 and CP2 with napin and cruciferin as major component, respectively. The protein conformation changes and interactions during gel formation were monitored by Fourier-transform infrared spectroscopy and advanced rheometer, and the protein network microstructures were observed using scanning electron microscopy. The results revealed that CP1 and CP2 exhibited different thermal and gelling properties due to their distinct molecular weight and amino acid composition. However, for both of them, lower heating temperature and pH only caused protein denaturation without splitting of disulfide bonds to produce randomly aggregated particulate fractal microstructure which was mainly stabilized by hydrophobic interactions. Whereas new gels with macro-porous dense wall structure and dramatically improved mechanical strength were prepared at high heating temperature and pH due to establishment of bridges between the interaction points on molecular chains. This generated knowledge has allowed preparation of canola protein gels with modulated mechanical properties by controlling the processing conditions, thus provided opportunities for canola protein to be used as new gelling reagent in both food and non-food applications.
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?
At high temperature (120°C) and pH 9-11, canola protein gels formed a macro-porous dense network structure with significantly higher gel strength than at low temperature and pH 5-7.
“In contrast, the macro-porous dense network structure was formed at high temperature (120°C) and pH 9-11, with the latter demonstrating significantly higher gel strength than the former.”
From A Review of Gelation of Plant Proteins and Their Influencing Factors (2025) · cites this paper as Yang et al. (2014)
At low temperature (80°C) and pH 5-7, canola protein gels exhibited a particulate fractal network structure characterized by randomly aggregated particles.
“Yang et al. (2014) found that at low temperature (80°C) and pH 5-7, canola protein gels exhibited a particulate fractal network structure characterized by randomly aggregated particles.”
From A Review of Gelation of Plant Proteins and Their Influencing Factors (2025) · cites this paper as Yang et al. (2014)
Cited by
Sorted by citations
Zhang, S., Huang, W., Feizollahi, E., Roopesh, M. S., & Chen, L. (2021) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2020.102567 · Cited by 188 · see citing works
Self-citationFabrication of pea protein gels with modulated rheological properties using high pressure processing
Zhang, S., Han, J., & Chen, L. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109002 · Cited by 53 · see citing works
Self-citationA Review of Gelation of Plant Proteins and Their Influencing Factors
Hui, D., Liang, W., Wang, R., Feng, X., & Tang, X. (2025) · Sustainable Food Proteins · doi:10.1002/sfp2.70037 · Cited by 12 · see citing works
Faure, R., Kapel, R., Marchal, P., Génin, G., & Beaubier, S. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.112100 · Cited by 2 · see citing works
- Authors
- Yang, C., Wang, Y., Vasanthan, T., & Chen, L.
- Affiliations
- University of Alberta (CA)
- Corresponding author
- Chen, Lingyun
- Venue
- Food Hydrocolloids
- Publisher
- Elsevier BV
- Published
- 2014-10
- Volume
- 40
- Pages
- 225-236
- ISSN
- 0268-005X (ISSN-L)
- OpenAlex
- W1978773013
- Cited by
- 98
- References
- 0
- Citations by year
- 2026: 9 · 2025: 12 · 2024: 14 · 2023: 12 · 2022: 7 · 2021: 11 · 2020: 8 · 2019: 8 · 2018: 5 · 2017: 4 · 2016: 4 · 2015: 4
- FWCI
- 5.73
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Food Hydrocolloids (publishedVersion)
- Funders
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- Alberta Crop Industry Development Fund Ltd. (ACIDF)
- Alberta Innovates Bio Solutions (AI Bio)
- Canada Foundation for Innovation (CFI)
- 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
- Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
- Keywords
- canola protein, protein gels, heat-induced gelation, pH effect, heating temperature, napin, cruciferin, protein denaturation, disulfide bond cleavage, hydrophobic interactions, gel microstructure, gel mechanical strength, gelling agents, protein conformation
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
