The DOI matches its Crossref record; 40 of the 41 references it cites were found in a registry or an index.
Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“Gels can be classified into transparent and opaque gels depending on the types of protein aggregates.Transparent gels are formed by fibrillar aggregates, while opaque gels are formed by particulate aggregates (Bryant and McClements 1998).”
From A Review of Gelation of Plant Proteins and Their Influencing Factors (2025) · cites this paper as Bryant and McClements 1998
In the citing paper
“Hydrophobic interactions play a major role in determining the conformation and interaction of protein molecules (Bryant and McClements, 1998”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Bryant and McClements, 1998
In the citing paper
“It should be noted that hydrophobic interactions increase up to a maximum at about 60 to 70°C, at which point they begin to slowly lose strength as the temperature is further increased (Bryant and McClements, 1998”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Bryant and McClements, 1998
In the citing paper
“Electrostatic repulsion increases with increasing temperature (Bryant and McClements, 1998”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Bryant and McClements, 1998
In the citing paper
“Hydrophobic interactions tend to increase in strength with temperature (Bryant and McClements, 1998”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Bryant and McClements, 1998
In the citing paper
“They manifest themselves as strong attractive forces between nonpolar groups separated by water.”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Bryant and McClements, 1998
Citations
Cites
Intermolecular and Surface Forces
(2011) · Elsevier eBooks · doi:10.1016/b978-0-12-391927-4.10024-6 · Cited by 17,242
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,829
Hydrogen bonding in globular proteins
Baker, E. N., & Hubbard, R. E. (1984) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(84)90007-5 · Cited by 1,860
Lumry, R. W., & Rajender, S. (1970) · Biopolymers · doi:10.1002/bip.1970.360091002 · Cited by 1,224
The colloidal domain: where physics, chemistry, biology, and technology meet
(1995) · Choice Reviews Online · doi:10.5860/choice.32-3315 · Cited by 1,130
An introduction to food colloids
(1992) · Choice Reviews Online · doi:10.5860/choice.30-2095 · Cited by 1,036
Némethy, G., & Scheraga, H. A. (1962) · The Journal of Physical Chemistry · doi:10.1021/j100816a004 · Cited by 974
Temperature dependence of the hydrophobic interaction in protein folding.
Baldwin, R. L. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8069 · Cited by 900
Ben-Naim, A. Y. (1980) · Springer eBooks · doi:10.1007/978-1-4684-3545-0 · Cited by 651
Proteins in Whey: Chemical, Physical, and Functional Properties
Kinsella, J. E., & Whitehead, D. M. (1989) · Advances in food and nutrition research · doi:10.1016/s1043-4526(08)60130-8 · Cited by 619
Research works printed but not linked: 6
- Kinsella, J.E. (1982) ‘Relationships Between Structure and Functional Properties of Food Proteins’ in Food Proteins (P.F. Fox and J.J. Condon, eds), pp. 51–103, Applied Science
- Kilara, A. and Harwalker, V.R. (1996) ‘Denaturation’ in Food Proteins: Properties and Characterization (S. Nakai and H.W. Modler, eds), pp. 71–135, VCH Publishers, Inc
- Koning, M.M.G. and Visser, H. (1992) in Protein Interactions (H. Visser, ed.) pp. 1–24, VCH Publishers
- Fennema, O.R. (1996) ‘Water and Ice’ in Food Chemistry (3rd edn.) (O.R. Fennema, ed.), pp. 17–94, Marcel Dekker, Inc
- Freidman, M. (1973) The Chemistry and Biochemistry of the Sulfhydril Group in Amino Acids, Peptides and Proteins, Pergamon Press
- Hvidt, A. and Westh, P. (1992) ‘Stabilization and Destabilization of Protein Conformations’ in Protein Interactions (H. Visser, ed.), pp. 327–343, VCH Publishers
Cited by
Sorted by citations
Items 601–643 of 643
de Andrade, I. M. G. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.74.2017.tde-01122017-144603
Effect of Chitosan and Sodium Tripolyphosphate on Gelling Properties of Pork Myofibrillar Protein
Jan, M. R., Ki, H. S., & Chi, K. B. (2014) · Journal of Agriculture Science & Technology · doi:10.29335/tals.2014.48.35
“일반적으로 단백질을 등전점에 근접하도록 pH를 저하시키면, 단백질의 전반적인 전하가 0에 도달하 며, 각 단백질간의 정전기적 척력이 최소화되기 때 문에 산성 겔을 형성할 수 있으며(Bryant and McClements, 1998), 이러한 낮은 pH 하에 가열 처리된 겔은 pH가 높은 단백질 겔에 비하여 상대 적으로 높은 겔 강도를 보인다고 보고되고 있다.”
Olivares, M., Pauletti, M. S., Costa, S. C., Vicin, D. A. D. P., & Rubiolo, A. C. (2014) · Latin American Applied Research - An international journal · doi:10.52292/j.laar.2014.439
Oat protein structure-function properties and value-added application
Nieto, N. (2015) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3t727m9s
Brito‐Oliveira, T. C. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.74.2017.tde-16082017-141101
Whey protein micro-particles as multifunctional materials for structure and delivery
Moakes, R. J. A. (2018) · University of Birmingham Institutional Research Archive (University of Birmingham)
Effects of structure on hydrogel microbead function
van Leusden, P. (2018) · doi:10.18174/446239
The Self-Organisation of Biological Soft matter Systems at Different Length-scales
Blumlein, A. (2016) · Maynooth University ePrints and eTheses Archive (Maynooth University)
Designing Biopolymer and Colloidal Systems
Michelon, M., Furtado, G. D. F., Mantovani, R. A., & Cunha, R. L. (2022) · Food engineering series · doi:10.1007/978-3-030-83570-5_2
Gelificação a frio de proteinas do soro do leite
Cavallieri, Â. L. F. (2007) · doi:10.47749/t/unicamp.2007.396094
Feichtinger, A., Giménez-Ribes, G., Landman, J., & Scholten, E. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111782
Vasconcelos, R. B., Sousa, R. R., Cavallini, G. S., Sarmento, R. A., & de Souza, N. L. G. D. (2025) · Polymer Engineering and Science · doi:10.1002/pen.70178
“Interactions due to van der Waals forces typically have bond energies ranging from 2.0 to 4.0 kJ/ mol, while hydrogen bonding, which may be within or close to chemical adsorption, has energy values ranging from 5 to 30 kJ/ mol or more [70, 71].”
InfluentialYu, F., You, X., Zhou, T., Jiang, H., Zhang, H., Zhang, X., & Wang, C. (2026) · Food Biophysics · doi:10.1007/s11483-026-10161-5
“Sulfhydryl groups are recognized as highly reactive func - tional groups within protein molecules, significantly influencing protein aggregation and dispersion [30].”
Water soaking improves pizza bake properties of fat-free mozzarella cheese shreds
Sutariya, S. G., & Salunke, P. (2025) · JDS Communications · doi:10.3168/jdsc.2025-0879
“Additionally, increased electrostatic repulsion and decreased hydrogen bonding further destabilize the matrix, shifting the balance toward weaker protein-protein interactions and promoting softening and melting (Bryant and McClements, 1998; Lucey et al., 2003).”
New water/water emulsions stabilized by Pickering effect
Gonzalez-Jordan, A. (2018) · doi:10.70675/6984da18z3dd0z4e90z8c50zfa932cd82be9
Ben-Harb, S. (2017) · theses.fr (ABES) · doi:10.70675/892eccefz40b0z4753z8851zf5dd6c53bdfe
Impact de la structure des aliments sur la biodisponibilité des micronutriments
Hiolle, M. (2019) · theses.fr (ABES) · doi:10.70675/fd44540czac6fz4725z8a8bz09af4feb0b3d
Calcium binding to β -lactoglobulin. Effects of pH and ionic strength.
Gillies, G., & Westberry, B. P. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.150229
Liu, T., Li, Z., Liu, M., Guan, T., Li, X., & Tang, Y. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.150555
Ubaid, M., & Saini, C. S. (2026) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2026.104734
Exploring a cold-gelled whey protein-based ink for applications in cultured meat 3D bioprinting
Zanderigo, G., Alicicco, G., Fiorati, A., Jacchetti, E., Raimondi, M. T., Mauri, E., Moscatelli, D., & Colosimo, B. M. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154479
Metadata
- Authors
- Bryant, C. M., & McClements, D. J.
- Affiliations
- University of Massachusetts Amherst (US)
- Corresponding author
- Bryant, Cory M
- ORCID
- McClements, D.Julian
- Venue
- Trends in Food Science & Technology
- Publisher
- Elsevier BV
- Published
- 1998-04
- Volume
- 9
- Issue
- 4
- Pages
- 143-151
- ISSN
- 0924-2244 (ISSN-L)
- OpenAlex
- W2034747455
- Cited by
- 643
- References
- 41
- Citations by year
- 2026: 16 · 2025: 19 · 2024: 25 · 2023: 21 · 2022: 20 · 2021: 34 · 2020: 29 · 2019: 41 · 2018: 40 · 2017: 36 · 2016: 34 · 2015: 38 · 2014: 37 · 2013: 36 · 2012: 37
- FWCI
- 13.95
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Food Science & Technology (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Keywords
- whey protein, cold-set gels, protein functional properties, emulsification, gelation, thickening, foaming, water holding capacity, functional food ingredients
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
