Cited by 643Proteins in Food SystemsProtein Structure and DynamicsPolysaccharides Composition and Applications

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Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey

Bryant, Cory M, McClements, D.Julian·1998·Trends in Food Science & Technology

DOI 10.1016/s0924-2244(98)00031-4

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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
Enthalpy–entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous properly of water
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
THE STRUCTURE OF WATER AND HYDROPHOBIC BONDING IN PROTEINS. III. THE THERMODYNAMIC PROPERTIES OF HYDROPHOBIC BONDS IN PROTEINS1,2
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
Hydrophobic Interactions
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

Show all 41 references

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

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“In this molten globule state, the free thiol group and part of the hydrophobic groups that were previously buried inside the globular structure are exposed and therefore available for reaction (Bryant and McClements, 1998).”
Background
Environmental parameters-dependent self-assembling behaviors of α-zein in aqueous ethanol solution studied by atomic force microscopy
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Fabrication, characterization and properties of filled hydrogel particles formed by the emulsion-template method
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Self-citation
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Milk proteins
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Self-citation
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“…the heated cheese mass (Relyveld 1977) or increased protein aggregation mediated by calcium phosphate complexes and/or through alteration in the proportions of different interactions (hydrophobic or electrostatic) (Bryant and McClements 1998; Jeurnink and de Kruif 1995; Marchesseau and Cuq 1995).”
Background
Ohmic vs. conventional heating: Influence of moderate electric fields on properties of egg white protein gels
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Self-citation
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Background
Effect of pH and Temperature on the Viscosity of Texturized and Commercial Whey Protein Dispersions
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“[2,3] The proteins act as good emulsifying, foaming, thickening, and gelling agents.[3,4] Modification of physicochemical characteristics of whey proteins, such as conformation, molecular interactions (hydrophobic, disulfide interchange, electrostatic interactions), and molecular weight, accomplished by changing the e…”
Background
Preparation and characterization of gellan gum microspheres containing a cold-adapted β-galactosidase from Rahnella sp. R3
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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)
DOI: 10.1016/s0924-2244(98)00031-4
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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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Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey

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