Cited by 727Proteins in Food SystemsMilk Quality and Mastitis in Dairy CowsAnimal Diversity and Health Studies

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Casein Interactions: Casting Light on the Black Boxes, the Structure in Dairy Products

Horne, David S.·1998·International Dairy Journal

DOI 10.1016/s0958-6946(98)00040-5

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Statistical theory of the adsorption of interacting chain molecules. 1. Partition function, segment density distribution, and adsorption isotherms
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On the Stability of Casein Micelles
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Casein sub-micelles: do they exist?
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pH-Induced dissociation of bovine casein micelles. II. Mineral solubilization and its relation to casein release
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Association of caseins and casein micelle structure.
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The voluminosity of bovine casein micelles and some of its implications
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“In the dual-binding model, calcium phosphate through binding to phosphoseryl clusters not only forms cross-links, but also reduce proteins charge, which makes the attractive interactions between hydrophobic regions a dominant force [8].”
Background
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“[24] and Horne [29], the calcium sensitivity of the different casein species is dependent on the concentration of phosphorylated amino acids in the primary structure, which increases from αS2 > αS1 > β > κ.”
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Rheological and sensory performance of a protein-based sweetener (MNEI), sucrose, and aspartame in yogurt
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Combined acid‐ and rennet‐induced gelation of a mixed soya milk–cow's milk system
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“Increased κ-CN content is related to an increased number of small micelles in κ-CN BB milk, which results in more compact curds (Horne, 1998) when milk is processed.”
Background
Protein Hydration and Viscosity of Dairy Fluids
Carr, A. J., Southward, C. R., & Creamer, L. K. (2003) · Springer eBooks · doi:10.1007/978-1-4419-8602-3_35 · Cited by 27
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Peng, Y., Horne, D. S., & Lucey, J. A. (2010) · Journal of Dairy Science · doi:10.3168/jds.2009-2792 · Cited by 27
“…the loss of CCP, but these casein particles are not completely dissociated by the loss of the CCP crosslinks because of the concurrent neutralization of the phosphoserine charges by the acid, thus maintaining an attractive interaction balance in favor of the hydrophobic interaction (Horne, 1998).”
BackgroundSelf-citation
Controlling the texture of fermented dairy products: the case of yoghurt
Jaros, D., & Rohm, H. (2003) · Elsevier eBooks · doi:10.1533/9781855737075.1.155 · Cited by 27
Impact of the structure of polyunsaturated soy phospholipids on the structural parameters and functionality of their complexes with covalent conjugates combining sodium caseinate with maltodextrins
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“The comparison of the measured both structural and thermodynamic parameters of the complex particles with those of the pure conjugates allow visualizing the formed complexes by the schematic representation based on the dual binding model of the casein micelles suggested by Horne (1998) (Tables 2, 4 and 5).”
Background
Distribution of Ca, P and Mg and casein micelle mineralisation in donkey milk from the second to ninth month of lactation
Malacarne, M., Criscione, A., Franceschi, P., Tumino, S., Bordonaro, S., Frangia, F. D., Marletta, D., & Summer, A. (2016) · International Dairy Journal · doi:10.1016/j.idairyj.2016.11.002 · Cited by 26
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Fantuz, F., Ferraro, S., Todini, L., Cimarelli, L., Fatica, A., Marcantoni, F., & Salimei, E. (2020) · Journal of Dairy Science · doi:10.3168/jds.2020-18251 · Cited by 26
“Aggregation of individual caseins into casein micelles occurs through a combination of hydrophobic interactions between hydrophobic regions of the caseins, and electrostatic interaction mediated by nanoclusters of calcium phosphate (known as colloidal calcium phosphate; CCP) sequestered in an amorphous form between ph…”
Background
Effect of spray freeze drying on the structural modification and rehydration characteristics of micellar casein powders
Ren, J., Liao, M., Ma, L., Chen, F., Liao, X., Hu, X., Miao, S., Fitzpatrick, J. J., & Ji, J. (2022) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2022.103093 · Cited by 26
Protein interactions and functionality of milk protein products
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Hussein, G., & Shalaby, S. M. (2014) · Annals of Agricultural Science Cairo · doi:10.1016/j.aoas.2014.06.004 · Cited by 33
“, 2003) and cause a weakening of the structural bonds (Horne, 1998).”
Background
Interactions between Adsorbed Layers of αS1-Casein with Covalently Bound Side Chains: A Self-Consistent Field Study
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Phase Stability of Concentrated Dairy Products
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“Aspects investigated include their detailed structure (Dalgleish, 1998), their size distribution (Holt, 1985), and the interactions between casein micelles (Holt and Horne, 1996; Horne, 1998; De Kruif, 1999), explaining the renneting and the acidification processes that are commonly used to”
Background
Structural, rheological and functional properties of extruded mozzarella cheese influenced by the properties of the renneted casein gels
Feng, R., van den Berg, F. W. J., Mokso, R., Lillevang, S. K., & Ahrné, L. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108322 · Cited by 25
“…i.e. EB + HB (21–32%), and calcium bridges i.e. CaB (30–59%), were the dominant interactions stabilizing the proteins in the curds, which were reported by previous work showing that these are the primary interactions influencing cheese melting behavior (Horne, 1998; Lucey, Johnson, & Horne, 2003).”
Background
Instantaneous gelation of acid milk gels via customized temperature-time profiles: Screening of concentration and pH suitable for temperature triggered gelation towards 3D-printing
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“[10, 12, 13] Their primary structure shows distinct hydrophilic and hydrophobic regions, which led to their consideration as diblock copolymers within the dual binding model of hydrophilic and hydrophobic interactions [14, 15].”
Background
Charge domain of modified pectins influence interaction with acidified caseins
Kim, Y., & Wicker, L. (2010) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2010.07.011 · Cited by 25
“The more linear self-assembly of a-S1,2-CSN, compared to b-CSN or k-CSN (Horne, 1998) most likely allows greater adsorption of pectin in the serum phase.”
BackgroundInfluential
Using Self-Consistent-Field Theory to Understand Enhanced Steric Stabilization by Casein-Like Copolymers at Low Surface Coverage in Mixed Protein Layers
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The Use of Lithium Chloride to Study Human Milk Micelles
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“acid residues. These interaction modes may be accommodated by different models for micelle structure ( Horne, 1998; Walstra, 1999).”
Background
Growth Kinetics and Fractal Dimensions of Casein Particles During Acidification
Chardot, V., Banon, S., Misiuwianiec, M., & Hardy, J. (2002) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(02)74046-0 · Cited by 24
“Acidification also induces the demineralization of casein micelles (Dalgleish and Law, 1989), with solubilization of calcium colloidal phosphate, which is an integral part of casein micelles (Walstra and Jenness, 1984; Horne, 1998; Walstra, 1999).”
Background
Characterisation of whey drainage kinetics during soft cheese manufacture in relation with the physicochemical and technological factors, pH at renneting, casein concentration and ionic strength of milk
Daviau, C., Pierre, A., Famelart, M., Goudédranche, H., Jacob, D., Garnier, M., & Maubois, J. (2000) · Le Lait · doi:10.1051/lait:2000135 · Cited by 24
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Assessing constituent volumes and morphology of bovine casein micelles using cryo-electron tomography
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Influence of calcium depletion on iron-binding properties of milk
Mittal, V. A., Ellis, A., Ye, A., Das, S., & Singh, H. (2015) · Journal of Dairy Science · doi:10.3168/jds.2014-8474 · Cited by 23
Characterisation of fractionated skim milk with small-angle X-ray scattering
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Liquid droplet-like behaviour of whole casein aggregates adsorbed on graphite studied by nanoindentation with AFM
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“Horne (1998) suggested a model, called dual binding (poly-condensation) model of the casein micelle.”
Background
Functional properties and biological activities of bovine casein proteins and peptides.
Darewicz, M., Dziuba, J., & Dziuba, M. (2006) · Conference Advance Technology · Cited by 23
Low molecular mass peptides generated by hydrolysis of casein impair rennet coagulation of milk
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“Moreover, many of the technologically important properties of milk, such as heat stability, rennet coagulability, and the strength and rennet-induced aggregation properties of rennet gels are strongly influenced by the calcium content of milk (Dalgleish & Corredig, 2012; Horne, 1998; Law & Tamime, 2010).”
Background
Fluorescein Thiocarbamoyl-Kappa-Casein Assay for the Specific Testing of Milk-Clotting Proteases
Ageitos, J. M., Vallejo, J. A., Poza, M., & Villa, T. G. (2006) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(06)72418-3 · Cited by 23
“Finally, the most recent model (Horne, 1998) proposes a double link among the caseins for gelling to take place.”
Background
Biopolymer nanovehicles for essential polyunsaturated fatty acids: Structure–functionality relationships
Semenova, M. G., Antipova, A. S., Zelikina, D. V., Martirosova, E. I., Plashchina, I. G., Palmina, N. P., Binyukov, V. I., Bogdanova, N. G., Kasparov, V. V., Mil, E., et al. (2016) · Food Research International · doi:10.1016/j.foodres.2016.05.008 · Cited by 23
Growth performance, nutrient utilisation and body composition of Macrobrachium rosenbergii fed graded levels of phytic acid
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Influence of ageing time on sodium caseinate gelation induced by glucono-δ-lactone at different temperatures
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Effect of Temperature and Aggregation Rate on the Fractal Dimension of Renneted Casein Aggregates
Vétier, N., Banon, S., Chardot, V., & Hardy, J. (2003) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(03)73844-2 · Cited by 23
Progress in Protein-Based Hydrogels for Flexible Sensors: Insights from Casein
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Changes in thermoviscoelastic and biochemical properties of Atroncau blancu and roxu Afuega'l Pitu cheese (PDO) during ripening
Piñeiro-Lago, L., Franco, I., & Tovar, C. A. (2020) · Food Research International · doi:10.1016/j.foodres.2020.109693 · Cited by 22
Current Major Advances in the Regulation of Milk Protein Gene Expression
Qian, X., & Zhao, F. (2014) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukaryotgeneexpr.2014012215 · Cited by 25
Comparison of re-micellised casein prepared from acid casein with micellar casein prepared by membrane filtration
Mounsey, J. S., O’Kennedy, B. T., & Kelly, P. M. (2005) · Le Lait · doi:10.1051/lait:2005022 · Cited by 22
Defining the conditions for heat-induced gelation of a caseinate-stabilized emulsion
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Solubility and structure of milk powders manufactured with the addition of disodium phosphate and tetrasodium pyrophosphate mixtures
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“Various molecular forces, including hydrophobic and electrostatic interactions, and colloidal calcium phosphate (ccp) maintain micelle cohesion.([5]) CCP is considered to be a cementing and neutralizing agent which contributes to micellar integrity and stability.”
Background
Amphiphilic copolymer stabilized core–shell structural casein-based emulsion
Ma, J., Gan, C., Xu, Q., Zhou, J., & Zhang, J. (2015) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2015.02.027 · Cited by 21
Calcium and phosphorus equilibria during acidification of skim milk at elevated temperature
Koutina, G., & Skibsted, L. H. (2015) · International Dairy Journal · doi:10.1016/j.idairyj.2015.01.006 · Cited by 20
Chemistry of Milk Constituents
Fox, P. F., Guinee, T. P., Cogan, T. M., & McSweeney, P. L. H. (2016) · Springer eBooks · doi:10.1007/978-1-4899-7681-9_4 · Cited by 21
Effect of Intrinsic Disorder and Self-Association on the Translational Diffusion of Proteins: The Case of α-Casein
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Characterising the influence of milk fat towards an application for extrusion-based 3D-printing of casein−whey protein suspensions via the pH−temperature-route
Daffner, K., Ong, L., Hanssen, E. G., Gras, S. L., & Mills, T. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.106642 · Cited by 21
Steady, dynamic, creep/recovery, and textural properties of yoghurt/molasses blends: Temperature sweep tests and applicability of Cox–Merz rule
Eroglu, A., Bayrambaş, K., Eroğlu, Z., Toker, Ö. S., Yılmaz, M. T., Karaman, S., & Doğan, M. (2015) · Food Science and Technology International · doi:10.1177/1082013214566478 · Cited by 21
Formation of Reconstituted Casein Micelles with Human β-Caseins and Bovine κ-Casein
Sood, S. M., Erickson, G., & Slattery, C. W. (2002) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(02)74097-6 · Cited by 21
“Recently, Tziboula and Horne (1999) examined the distribution of caseins in the micelles of goat milks, including one in which the αs1-CN was a mutant (variant F) with 37 residues deleted, including five phosphoserines.”
Background
Acid Coagulation of Milk
Lucey, J. A., & Singh, H. (2003) · Springer eBooks · doi:10.1007/978-1-4419-8602-3_28 · Cited by 22
Understanding temperature-sensitive caseinate emulsions: new information from diffusing wave spectroscopy
Eliot, C., Horne, D. S., & Dickinson, E. (2004) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2004.06.005 · Cited by 21
Self-citation
Influence of Processing on Rheological and Textural Characteristics of Goat and Sheep Milk Beverages and Methods of Analysis
da Silva, V. B., & da Costa, M. P. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-815259-1.00011-2 · Cited by 20
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Casein Aggregates Built Step-by-Step on Charged Polyelectrolyte Film Surfaces Are Calcium Phosphate-cemented
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“Self-association of a- and b-caseins may form worm-like polymeric chains and hedgehog-like micelles, respectively (Horne, 1998).”
Background
Effect of tetrasodium pyrophosphate concentration and cooking time on the physicochemical properties of process cheese
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“Casein interactions can be viewed as a balance between attractive and repulsive forces (Horne, 1998).”
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The effect of transglutaminase treatment on the physico-chemical properties of skim milk with added ethylenediaminetetraacetic acid
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Cheddar Cheese and Related Dry-Salted Cheese Varieties
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Effect of Tetrasodium Pyrophosphate on the Physicochemical Properties of Yogurt Gels
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“Calcium chelating agents disrupt casein micelles because colloidal calcium phosphate ( CCP ) is a key structural or cross-linking unit in micelles (Horne, 1998).”
BackgroundSelf-citation
Mesoscale crystallization of calcium phosphate nanostructures in protein (casein) micelles
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Chymosin in Cheese Making
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Molecular Mobility in Dense Protein Systems: An Investigation through 1H NMR Relaxometry and Diffusometry
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Influence of heat on miscibility of Quillaja saponins in mixtures with a co-surfactant
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Natural Polymers: Their Blends, Composites and Nanocomposites: State of Art, New Challenges and Opportunities
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Adsorption and Dilational Rheology of Mixed β-Casein/DoTAB Layers Formed by Sequential and Simultaneous Adsorption at the Water/Hexane Interface
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“bilizing the CN micelle according to accepted models (Horne, 1998), hydropathy plots were used.”
Cheese | Rennet-Induced Coagulation of Milk
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Implications of kappa-casein evolutionary diversity for the self-assembly and aggregation of casein micelles
Manguy, J., & Shields, D. C. (2019) · Royal Society Open Science · doi:10.1098/rsos.190939 · Cited by 18
“Two models of casein micelle formation have been proposed, one suggesting that polar interactions may be critical [25], and the other placing a greater emphasis on hydrophobic interactions [26].”
Background
Effect of a low temperature step during fermentation on the physico-chemical properties of fat-free yogurt
Trejo, R., Corzo‐Martínez, M., Wilkinson, S., Higginbotham, K. L., & Harte, F. (2013) · International Dairy Journal · doi:10.1016/j.idairyj.2013.12.003 · Cited by 18

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)
DOI: 10.1016/s0958-6946(98)00040-5
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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 › Animal Science and Zoology › 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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