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
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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
Food protein-based materials as nutraceutical delivery systems
Chen, L., Remondetto, G. E., & Subirade, M. (2006) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2005.12.011 · Cited by 1,183
“egg white, soybean, and whey proteins) has attracted much attention over the years because of its physicochemical and industrial significance (Bryant and McClement, 1998; Clark, Kavanagh, & Ross-Murphy, 2001; Clark & Ross-Murphy, 1987; Ziegler & Foegeding 1990).”
BackgroundInvited review: perspectives on the basis of the rheology and texture properties of cheese.
Lucey, J. A., Johnson, M. E., & Horne, D. S. (2003) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(03)73869-7 · Cited by 723
β-Lactoglobulin and WPI aggregates: Formation, structure and applications
Nicolaï, T., Britten, M., & Schmitt, C. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.02.006 · Cited by 575
Mezzenga, R., & Fischer, P. (2013) · Reports on Progress in Physics · doi:10.1088/0034-4885/76/4/046601 · Cited by 560
“Furthermore, in addition to these potentials, other interactions play an important role in the phase behavior of proteins: hydrophobic interactions, hydration, solvation and hydrogen bonds, hydrophilic interaction, charge residues complementarity, salt specificity effects and molecular recognition all contribute to in…”
BackgroundEffect of ultrasound treatment on solubility and foaming properties of whey protein suspensions
Jambrak, A. ., Mason, T. J., Lelas, V., Herceg, Z., & Herceg, I. L. (2007) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2007.10.004 · Cited by 550
“Whey are widely used as ingredients in foods due to their unique functional properties, i.e. emulsification, gelation, thickening, foaming, and fat and flavor binding capacity (Bryant and McClements, 1998; McClements, 1995; Mason, 1998).”
Background
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
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