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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“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
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“Since electrostatic repulsions are shielded by ions in the solution (Bryant & McClements, 1998; Renard et al., 1999), it is much easier for the MPWPC to approach each other and flocculate again when salt is present.”
BackgroundBehavior of Protein in the Presence of Calcium during Heating of Whey Protein Concentrate Solutions
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“The production of gels can be induced by heat, at a temperature of about 90 ◦C, for 5 min, or by lowering the pH by adding glucono-δ-lactone (GDL) leading to acid induced gels that can be commercialized for incorporating in various products, such as mayonnaises, yoghurts, desserts, giving them improved functional prop…”
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“…cold gelation of heated protein solutions has been reported for some proteins, such as whey protein concentrates, whey protein isolates and b-lactoglobulin (Barbut & Foegeding, 1993; Bryant & McClements, 1998; Elofsson, Dejmek, Paulsson, & Burling, 1997; Ju & Kilara, 1998; ax: þ55 (31) 38992208.”
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“As reviewed by Bryant and McClements (1998) salt was mainly used to induce gelation.”
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“Some of the weakening of gels with increasing temperature could also be due to the decrease in strength of hydrogen bonds (Bryant and McClements, 1998).”
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“Hydrophobic interactions, which tend to increase in strength with temperature (Bryant and McClements, 1998), can also influence melting.”
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Hemp globulin forms colloidal nanocomplexes with sodium caseinate during pH-cycling
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Rheological and microstructural properties of Bambara groundnut protein gels
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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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