Casein interactions: Casting light on the Black Boxes, the structure in dairy products
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In the dual-binding model, κ-CN can link only to a hydrophobic residue on another CN molecule; because it has no phosphoseryl cluster, the polymer chain ends there, and the proportion of κ-CN limits the micelle size.
“κ-Casein, however, can link only to a hydrophobic residue on another CN molecule. Because it has no phosphoseryl cluster to permit further extension, the polymer chain ends there. No further growth occurs beyond this point. This occurs for each growing chain and hence the proportion of κ-CN limits the micelle size.”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Horne, 1998
In the dual-binding model, κ-CN acquires an external surface position where it acts as a steric stabilizer.
“In consequence, the κ-CN acquires an external surface position where it acts as a steric stabilizer.”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Horne, 1998
Decreasing hydrophobic interaction by lowering temperature or increasing electrostatic repulsion by dissolving out Ca phosphate but maintaining pH disrupts one bonding pathway, weakens adjacent bonds, and causes (partial) disintegration of the micelle.
“Decreasing hydrophobic interaction by lowering temperature or increasing electrostatic repulsion by dissolving out Ca phosphate but maintaining pH, disrupts one bonding pathway, weakens also those adjacent bonds and causes (partial) disintegration of the micelle.”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Horne, 1998
The solubility of Ca and the CCP equilibrium are dependent on temperature.
“The solubility of Ca and the CCP equilibrium are also dependent on temperature (Horne, 1998”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Horne, 1998
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Self-citationBeliciu, C. M., & Moraru, C. I. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.01.011 · Cited by 112 · see citing works
Acid and rennet-induced coagulation behavior of casein micelles with modified structure
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Effect of Calcium Concentration on the Structure of Casein Micelles in Thin Films
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Casein Proteins: Structural and Functional Aspects
Bhat, M. Y., Dar, T. A., & Singh, L. R. (2016) · InTech eBooks · doi:10.5772/64187 · Cited by 109 · see citing works
Revisiting the interpretation of casein micelle SAXS data
Ingham, B., Smialowska, A., Erlangga, G. D., Matia‐Merino, L., Kirby, N. M., Wang, C., Haverkamp, R., & Carr, A. J. (2016) · Soft Matter · doi:10.1039/c6sm01091a · Cited by 108 · see citing works
Dickinson, E., Radford, S. J., & Golding, M. (2003) · Food Hydrocolloids · doi:10.1016/s0268-005x(02)00055-3 · Cited by 108 · see citing works
Milk Salts: Technological Significance
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Self-citationCasein micelle structure: a concise review
Phadungath, C. (2005) · DOAJ (DOAJ: Directory of Open Access Journals) · Cited by 105 · see citing works
Acidified sodium caseinate emulsion foams containing liquid fat: A comparison with whipped cream
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The composition and physico-chemical properties of human milk: A review
Meng, F., Uniacke‐Lowe, T., Ryan, C. A., & Kelly, A. L. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.03.040 · Cited by 112 · see citing works
Properties of Milk Protein Gels Formed by Phosphates
Mizuno, R., & Lucey, J. A. (2007) · Journal of Dairy Science · doi:10.3168/jds.2007-0229 · Cited by 103 · see citing works
Bovine β-casein: Isolation, properties and functionality. A review
Atamer, Z., Post, A. E., Schubert, T., Holder, A., Boom, R. M., & Hinrichs, J. (2016) · International Dairy Journal · doi:10.1016/j.idairyj.2016.11.010 · Cited by 104 · see citing works
Texture of Low-Fat Iranian White Cheese as Influenced by Gum Tragacanth as a Fat Replacer
Rahimi, J., Khosrowshahi, A., Madadlou, A., & Aziznia, S. (2007) · Journal of Dairy Science · doi:10.3168/jds.2007-0121 · Cited by 101 · see citing works
Effect of Trisodium Citrate on Rheological and Physical Properties and Microstructure of Yogurt
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Self-citationThe Syneresis of Rennet-coagulated Curd
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The Impact of Seasonality in Pasture-Based Production Systems on Milk Composition and Functionality
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Size distribution of pressure-decomposed casein micelles studied by dynamic light scattering and AFM
Gebhardt, R., Doster, W., Friedrich, J., & Kulozik, U. (2006) · European Biophysics Journal · doi:10.1007/s00249-006-0058-6 · Cited by 100 · see citing works
Casein micelle structure and stability
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Self-citationPerspectives on casein interactions
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Self-citationInfluence of micellar calcium and phosphorus on rennet coagulation properties of cows milk
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Preparation and evaluation of hemicellulose films and their blends
Mendes, F. R. D. S., Bastos, M. D. S. R., Mendes, L. G., Silva, Â. R. A., de Sousa, F. D., Monteiro‐Moreira, A. C. D. O., CHENG, H. N., Biswas, A., & Moreira, R. D. A. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.03.037 · Cited by 98 · see citing works
Formation, Structural Properties, and Rheology of Acid-Coagulated Milk Gels
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Anema, S. G. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-374039-7.00008-8 · Cited by 95 · see citing works
Lucey, J. A. (2015) · Springer eBooks · doi:10.1007/978-1-4939-2800-2_12 · Cited by 95 · see citing works
Du, B., Li, J., Zhang, H., Long, H., Chen, P., & Zhou, J. (2008) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2008.10.004 · Cited by 94 · see citing works
AFM Imaging of Milk Casein Micelles: Evidence for Structural Rearrangement upon Acidification
Ouanezar, M., Guyomarc’H, F., & Bouchoux, A. (2012) · Langmuir · doi:10.1021/la3001448 · Cited by 92 · see citing works
Studies of casein micelle structure: the past and the present
Qi, P. X. (2007) · Le Lait · doi:10.1051/lait:2007026 · Cited by 91 · see citing works
- Authors
- Horne, D. S.
- Affiliations
- Hannah Research Foundation (GB)
- Corresponding author
- Horne, David S.
- ORCID
- Horne, David S.
- Venue
- International Dairy Journal
- Publisher
- Elsevier BV
- Published
- 1998-03
- Volume
- 8
- Issue
- 3
- Pages
- 171-177
- ISSN
- 0958-6946 (ISSN-L)
- OpenAlex
- W2168769318
- Cited by
- 723
- References
- 38
- Citations by year
- 2026: 13 · 2025: 25 · 2024: 33 · 2023: 31 · 2022: 16 · 2021: 24 · 2020: 27 · 2019: 34 · 2018: 24 · 2017: 38 · 2016: 28 · 2015: 31 · 2014: 32 · 2013: 30 · 2012: 42
- FWCI
- 12.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- International Dairy Journal (publishedVersion)
- Funders
- European Commission
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Agronomy and Crop Science › Milk Quality and Mastitis in Dairy Cows
- Life Sciences › Agricultural and Biological Sciences › Food Science › Animal Diversity and Health Studies
- Keywords
- casein micelles, hydrophobic interactions, electrostatic repulsion, calcium-induced aggregation, acid coagulation, ionic strength effects, temperature effects, pH effect, viscoelasticity, dairy products
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