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.
“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
Hydrophobic interactions play a major role in determining the conformation and interaction of protein molecules.
“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
Hydrophobic interactions increase up to a maximum at about 60 to 70°C, at which point they begin to slowly lose strength as temperature is further increased.
“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
Electrostatic repulsion increases with increasing temperature.
“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
Hydrophobic interactions tend to increase in strength with temperature.
“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
Hydrophobic interactions manifest as strong attractive forces between nonpolar groups separated by water.
“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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A New Multistep Ca2+-Induced Cold Gelation Process for β-Lactoglobulin
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Encapsulation of α-tocopherol in protein-based delivery particles
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- 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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