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

The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.

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

Open this paper in CoChat — free account

Integrity signals

Registry

Crossref · 10.1016/s0958-6946(98)00040-5

Cites

37 of 37 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Statistical theory of the adsorption of interacting chain molecules. 1. Partition function, segment density distribution, and adsorption isotherms
Scheutjens, J. M. H. M., & Fleer, G. J. (1979) · The Journal of Physical Chemistry · doi:10.1021/j100475a012 · Cited by 1,348
Statistical theory of the adsorption of interacting chain molecules. 2. Train, loop, and tail size distribution
Scheutjens, J. M. H. M., & Fleer, G. J. (1980) · The Journal of Physical Chemistry · doi:10.1021/j100439a011 · Cited by 967
On the Stability of Casein Micelles
Walstra, P. (1990) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(90)78875-3 · Cited by 558
Casein sub-micelles: do they exist?
Walstra, P. (1999) · International Dairy Journal · doi:10.1016/s0958-6946(99)00059-x · Cited by 343
pH-Induced dissociation of bovine casein micelles. I. Analysis of liberated caseins
Dalgleish, D. G., & Law, A. J. R. (1988) · Journal of Dairy Research · doi:10.1017/s0022029900033306 · Cited by 294
pH-Induced dissociation of bovine casein micelles. II. Mineral solubilization and its relation to casein release
Dalgleish, D. G., & Law, A. J. R. (1989) · Journal of Dairy Research · doi:10.1017/s0022029900029290 · Cited by 292
Casein micelle interactions
de Kruif, C. G. (1999) · International Dairy Journal · doi:10.1016/s0958-6946(99)00058-8 · Cited by 273
Association of caseins and casein micelle structure.
Schmidt, D. G. (1982) · Cited by 246
The hairy casein micelle: evolution of the concept and its implications for dairy technology
Holt, C., & Horne, D. S. (1996) · Netherlands milk and dairy journal · Cited by 211
Self-citation
The voluminosity of bovine casein micelles and some of its implications
Walstra, P. (1979) · Journal of Dairy Research · doi:10.1017/s0022029900017234 · Cited by 175

Show all 38 references

Sorted by citations

Items 401–500 of 727

Structural changes of casein micelles in a rennin gradient film with simultaneous consideration of the film morphology
Gebhardt, R., Roth, S. V., Burghammer, M. C., Riekel, C., Tolkach, A., Kulozik, U., & Müller‐Buschbaum, P. (2009) · International Dairy Journal · doi:10.1016/j.idairyj.2009.10.004 · Cited by 18
Major Role of Voluminosity in the Compressibility and Sol–Gel Transition of Casein Micelle Dispersions Concentrated at 7 °C and 20 °C
Doudiès, F., Arsène, A.-S., Garnier-Lambrouin, F., Famelart, M., Bouchoux, A., Pignon, F., & Gésan-Guiziou, G. (2019) · Foods · doi:10.3390/foods8120652 · Cited by 18
Probing the structure-holding interactions in cheeses by dissociating agents – A review and an experimental evaluation with emmental cheese
Vilela, T. P., Gomes, A., & Ferreira, J. P. (2020) · Current Research in Food Science · doi:10.1016/j.crfs.2020.07.001 · Cited by 18
“In gel-like systems based on casein, such as cheese, literature proposes that self-association of casein micelles is also driven by different interactions, such as hydrophobic interactions and electrostatic ones (Horne, 1998).”
Background
Structural characterization of casein micelles: shape changes during film formation
Gebhardt, R., Vendrely, C., & Kulozik, U. (2011) · Journal of Physics Condensed Matter · doi:10.1088/0953-8984/23/44/444201 · Cited by 18
Protein content affects caramel processing and properties
Mendenhall, H., & Hartel, R. W. (2016) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2016.04.013 · Cited by 18
Cheese Microstructure 1
Everett, D. W., & Auty, M. A. E. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-417012-4.00021-1 · Cited by 18
Ultrasonic monitoring of yoghurt formation by using AT-cut quartz: Lighting of casein micelles interactions process during the acidification
Ehssein, C. O., Serfaty, S., Griesmar, P., Huérou, J. Y. L., Caplain, E., Martinez, L., Wilkie-Chancellier, N., & Gindre, M. (2006) · Ultrasonics · doi:10.1016/j.ultras.2006.05.034 · Cited by 18
Milk Proteins: Functionality and Use in Food Industry
Andiç, S., & Boran, G. (2015) · doi:10.1002/9781119108580.ch8 · Cited by 18
Minerals to dairy cows with focus on calcium and magnesium balance
Kronqvist, C. (2011) · Epsilon Open Archive (Sveriges lantbruksuniversitet biblioteket (Swedish University of Agricultural Sciences)) · Cited by 18
Formation by high power ultrasound of aggregated emulsions stabilised with milk protein concentrate (MPC70)
Zhang, R., Luo, L., Yang, Z., Ashokkumar, M., & Hémar, Y. (2021) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2021.105852 · Cited by 17
Interpreting the “twice gelation” mechanism of a novel egg-based yoghurt through the dynamics of rheology, microstructure, and intermolecular forces
Zang, J., You, H., Li, S., Zhang, Y., Xu, H., Tang, D., Shao-fu, W., Yao, Y., Tu, Y., & Yin, Z. (2023) · Food Bioscience · doi:10.1016/j.fbio.2023.103318 · Cited by 17
Comparison of Milk Kefirs Obtained from Cow’s, Ewe’s and Goat’s Milk: Antioxidant Role of Microbial-Derived Exopolysaccharides
M’hir, S., Ayed, L., Pasquale, I. D., Fanizza, E., Tlais, A. Z. A., Comparelli, R., Verni, M., Latronico, R., Gobbetti, M., Cagno, R. D., et al. (2024) · Antioxidants · doi:10.3390/antiox13030335 · Cited by 17
Structural and thermodynamic properties underlying the novel functionality of sodium caseinate as delivery nanovehicle for biologically active lipids
Semenova, M. G., Antipova, A. S., Belyakova, L. E., Polikarpov, Y. N., Anokhina, M. S., Grigorovich, N. V., & Моисеенко, Д. В. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.03.028 · Cited by 17
Impact of Cationic Surfactant on the Self-Assembly of Sodium Caseinate
Vinceković, M., Ćurlin, M., & Jurašin, D. D. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf5016472 · Cited by 17
Characterisation of African elephant beta casein and its relevance to the chemistry of caseins and casein micelles
Madende, M., Kemp, G., Stoychev, S., & Osthoff, G. (2018) · International Dairy Journal · doi:10.1016/j.idairyj.2018.05.013 · Cited by 17
Using the USAXS technique to reveal the fat globule and casein micelle structures of bovine dairy products
Peyronel, F., Marangoni, A. G., & Pink, D. A. (2019) · Food Research International · doi:10.1016/j.foodres.2019.108846 · Cited by 17
Determination of plasmin in milk using QCM and ELISA methods
Poturnayová, A., Szabo, K., Tatarko, M., Hucker, A., Kocsis, R., & Hianik, T. (2020) · Food Control · doi:10.1016/j.foodcont.2020.107774 · Cited by 17
“In addition, in the milk, the casein micelles contain also κ-casein, which is less cleaved in comparison with β-casein (Horne, 1998; Tatarko et al., 2018).”
Background
Effect of insoluble calcium concentration on endogenous syneresis rate in rennet-coagulated bovine milk
Choi, J., Horne, D. S., & Lucey, J. A. (2015) · Journal of Dairy Science · doi:10.3168/jds.2015-9527 · Cited by 17
“In Horne’s dual-bonding model for the structure of CM (Horne, 1998), CCP is an important material that supports the integrity of CM.”
BackgroundSelf-citation
The sol–gel transition temperature of skim milk concentrated by microfiltration as affected by pH and protein content
Schäfer, J., Läufle, I., Schmidt, C. M., Atamer, Z., Nöbel, S., Sonne, A., Kohlus, R., & Hinrichs, J. (2017) · International Journal of Dairy Technology · doi:10.1111/1471-0307.12488 · Cited by 17
Role of electrostatic interactions in the curd of Emmental cheese
Gagnaire, V., Trotel, E., Graët, Y. L., & Léonil, J. (2002) · International Dairy Journal · doi:10.1016/s0958-6946(02)00052-3 · Cited by 17
Constituents and Properties of Milk from Different Species
Huppertz, T., Upadhyay, V. K., Kelly, A. L., & Tamime, A. Y. (2006) · Wiley eBooks · doi:10.1002/9780470995860.ch1 · Cited by 18
USANS and SANS investigations on the coagulation of commercial bovine milk: Microstructures induced by calf and fungal rennet
Callaghan-Patrachar, N., Peyronel, F., Pink, D. A., Marangoni, A. G., & Adams, C. P. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.106622 · Cited by 16
Modelling and computer simulation of food structures
Euston, S. R. (2013) · Elsevier eBooks · doi:10.1533/9780857098894.2.336 · Cited by 16
Affinity of Microbial Transglutaminase to αs1-, β-, and Acid Casein under Atmospheric and High Pressure Conditions
Menéndez, O., Schwarzenbolz, U., Partschefeld, C., & Henle, T. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf8034447 · Cited by 16
Dairy Products
Hill, A. R., & Kethireddipalli, P. (2012) · Elsevier eBooks · doi:10.1016/b978-0-08-091809-9.00008-x · Cited by 18
Calcium effect on the swelling behaviour and stability of casein microparticles
Schulte, J., Stöckermann, M., Thill, S., & Gebhardt, R. (2020) · International Dairy Journal · doi:10.1016/j.idairyj.2020.104692 · Cited by 16
Milk protein gels
Lucey, J. A. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815251-5.00016-5 · Cited by 16
Casein Nomenclature, Structure, and Association
Rocha-Mendoza, D., & Jiménez‐Flores, R. (2021) · Encyclopedia of Dairy Sciences · doi:10.1016/b978-0-12-818766-1.00277-4 · Cited by 16
The effect of microbial transglutaminase on the immunoreactive and sensory properties of fermented milk beverages
Wróblewska, B., Kaliszewska‐Suchodoła, A., Kołakowski, P., & Troszyńska, A. (2012) · International Journal of Food Science & Technology · doi:10.1111/ijfs.12054 · Cited by 15
Monitoring the progression of calcium and protein solubilisation as affected by calcium chelators during small-scale manufacture of casein-based food matrices
McIntyre, I., O’Sullivan, M., & O’Riordan, D. (2017) · Food Chemistry · doi:10.1016/j.foodchem.2017.05.149 · Cited by 15
Review on mechanisms leading to fouling and stability issues related to heat treatment of casein-based RTD beverages
Abdallah, M., Scudeller, L. A., Hiolle, M., Lesur, C., Baniel, A., & Delaplace, G. (2022) · Food and Bioproducts Processing · doi:10.1016/j.fbp.2022.09.009 · Cited by 15
Invited review: Modeling milk stability
Holt, C., & Carver, J. A. (2024) · Journal of Dairy Science · doi:10.3168/jds.2024-24779 · Cited by 15
Functional and Bioactive Benefits of Selected Microalgal Hydrolysates Assessed In Silico and In Vitro
Hayes, M., Mora, L., Marzocchella, A., Kuchendorf, C. M., Ackermann, B., & Aurino, E. (2025) · Marine Drugs · doi:10.3390/md23020053 · Cited by 17
“The values obtained for the Chlorella mix and Scenedesmus mix hydrolysates in this study compare favorably (1.83 g of water/g of protein hydrolysate and 1.78 g of water/g of protein hydrolysate) [62].”
Influential
Comparative genomics of casein genes
Madende, M., & Osthoff, G. (2019) · Journal of Dairy Research · doi:10.1017/s0022029919000414 · Cited by 14
Compositional changes of casein micelles induced by calcium or chelatant addition at threefold and natural casein concentration
Reiter, M., Reitmaier, M., & Kulozik, U. (2022) · International Dairy Journal · doi:10.1016/j.idairyj.2022.105365 · Cited by 15
Study of chymosin hydrolysis of casein micelles under ultra high pressure: Effect on re-association upon pressure release
Heinrich, M. R., & Kulozik, U. (2011) · International Dairy Journal · doi:10.1016/j.idairyj.2011.02.003 · Cited by 15
Phase behaviour of casein micelles and barley beta-glucan polymer molecules in dietary fibre-enriched dairy systems
Repin, N. V., Scanlon, M. G., & Fulcher, R. G. (2012) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2012.02.021 · Cited by 15
The effect of transglutaminase on reconstituted skim milks at alkaline pH
Lam, E., McKINNON, I. R., Marchesseau, S., Otter, D. E., Zhou, P., & Hémar, Y. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.06.047 · Cited by 15
Effect of Reducing Agent TCEP on Translational Diffusion and Supramolecular Assembly in Aqueous Solutions of α-Casein
Melnikova, D. L., Skirda, V. D., & Nesmelova, I. V. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b12511 · Cited by 15
Basic Biochemical Properties of Recombinant Chymosins (Review)
Belenkaya, S. V., Балабова, Д. В., Belov, A. N., Koval, A. D., Щербаков, Д. Н., & Elchaninov, V. V. (2020) · Applied Biochemistry and Microbiology · doi:10.1134/s0003683820040031 · Cited by 15
κ-Casein Interactions in the Suspension of the Two Major Calcium-Sensitive Human β-Caseins
Sood, S. M., Erickson, G., & Slattery, C. W. (2003) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(03)73818-1 · Cited by 15
“recent so-called “dual-binding” model of Horne (1998).”
Background
Higher Order Structures of the Caseins: A Paradox?
Farrell, H. M., Brown, E. M., Hoagland, P. D., & Malin, E. L. (2003) · Springer eBooks · doi:10.1007/978-1-4419-8602-3_4 · Cited by 15
Structuring Dairy Products by Means of Processing and Matrix Design
Kulozik, U. (2007) · Springer eBooks · doi:10.1007/978-0-387-71947-4_19 · Cited by 15
“Various models exist to characterise the inner structure of the casein micelle (Phandungath 2005), so-called coat–core models, subunit models and internal structure models, the most widely accepted ones being the so-called sub-micelle model first established by Morr (1967) and the calcium–phosphate cluster model estab…”
Method
Milk Proteins | Casein Nomenclature, Structure, and Association
Farrell, H. M. (2011) · Encyclopedia of Dairy Sciences · doi:10.1016/b978-0-12-374407-4.00430-1 · Cited by 15
Unveiling the structure of the primary caseinate particle using small-angle X-ray scattering and simulation methodologies
Sun, Y., Tai, Z., Yan, T., Dai, Y., Hémar, Y., & Li, N. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110653 · Cited by 14
Stability of casein micelles subjected to CO2 reversible acidification: Impact of carbonation temperature and chilled storage time
Raouche, S., Dobenesque, M., Bot, A., Cuq, J.-L., & Marchesseau, S. (2007) · International Dairy Journal · doi:10.1016/j.idairyj.2007.07.007 · Cited by 14
Effects of Adding Low Levels of a Disulfide Reducing Agent on the Disulfide Interactions of β-Lactoglobulin and κ-Casein in Skim Milk
Nguyen, N. H. A., Wong, M., Anema, S. G., Havea, P., & Guyomarc’H, F. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf205297p · Cited by 14
Effect of high pressure processing on milk coagulation properties
Liepa, M., Zagorska, J., & Galoburda, R. (2017) · Research for Rural Development/Research for Rural Development (Online) · doi:10.22616/rrd.23.2017.033 · Cited by 14
“In a model of the casein micelle, colloidal calcium phosphate crosslinks the sub-micelles caseins and neutralises negatively charged phosphoserine groups, allowing the formation of hydrophobic interactions between caseins (Horne, 1998).”
Background
Effect of transglutaminase and acidification temperature on the gelation of reconstituted skim milk
Lam, E., Otter, D. E., Huppertz, T., Zhou, P., & Hémar, Y. (2019) · International Dairy Journal · doi:10.1016/j.idairyj.2019.01.006 · Cited by 14
Spontaneous aggregation of bovine milk casein micelles: Ultra-small angle x-ray scattering and mathematical modeling
Pink, D. A., Peyronel, F., Quinn, B. E., & Marangoni, A. G. (2019) · Physics of Fluids · doi:10.1063/1.5100161 · Cited by 14
Manufacture and Physicochemical Properties of Chitosan Oligosaccharide/A2 β-Casein Nano-Delivery System Entrapped with Resveratrol
Kim, M. Y., Ha, H., Istifiani, L. A., Han, K., Lee, W.-J., & Lee, M.-R. (2019) · Food Science of Animal Resources · doi:10.5851/kosfa.2019.e74 · Cited by 14
Heat-induced changes in dairy products containing sucrose
Rozycki, S., Buera, M. D. P., & Pauletti, M. S. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2009.04.096 · Cited by 14
The caseins
Fox, P. F., & Kelly, A. L. (2004) · Elsevier eBooks · doi:10.1533/9781855738379.1.29 · Cited by 14
The effect of dephosphorylation on the properties of αS1-casein enriched protein
Sun, X., Anema, S. G., & Gerrard, J. A. (2023) · International Dairy Journal · doi:10.1016/j.idairyj.2023.105744 · Cited by 13
Structure of biomimetic casein micelles: Critical tests of the hydrophobic colloid and multivalent-binding models using recombinant deuterated and phosphorylated β-casein
Raynes, J. K., Mata, J. P., Wilde, K. L., Carver, J. A., Kelly, S. M., & Holt, C. (2024) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2024.100096 · Cited by 13
“…of the more hydrophobic caseins in the interior of casein micelles and forms a steric barrier to prevent aggregation of the whole micelle (Holt and Horne, 1996; Horne, 1998; Linderstr ø m Lang, 1929; Payens, 1966; Slattery and Evard, 1973; Tuinier and de Kruif, 2002; Walstra, 1990; Waugh, 1971).”
Background
Current concepts of casein and casein micelle structure, interactions, and dynamics
Carver, J. A., & Holt, C. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15836-0.00002-0 · Cited by 13
Tuning the structure and coagulation behaviour of artificial casein micelles by varying the casein composition
Antuma, L. J., Boom, R. M., & Keppler, J. K. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111136 · Cited by 13
Rheology of rennet induced curd made from buffalo milk
Hussain, I., Grandison, A. S., & Bell, A. E. (2012) · The Journal of Animal and Plant Sciences · Cited by 13
Chapter 6 – Casein Micelle Structure and Stability
Horne, D. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405171-3.00006-4 · Cited by 15
Self-citation
Aggregation in a concentrated model protein system: a mesoscopic simulation of β-casein self-assembly
Dickinson, E., & Krishna, S. (2001) · Food Hydrocolloids · doi:10.1016/s0268-005x(00)00057-6 · Cited by 13
The influence of alkaline earth metal equilibria on the rheological properties of rennet-induced skim milk gels
Cooke, D. R., & McSweeney, P. L. H. (2014) · Dairy Science and Technology · doi:10.1007/s13594-014-0166-5 · Cited by 13
“These nanoclusters are involved in ionic attraction with numerous phosphoserine centers on casein molecules and represent an important structural component of the casein micelle (Horne 1998).”
Background
Calcium reduced skim milk retentates obtained by means of microfiltration
Schäfer, J., Mesch, I., Atamer, Z., Nöbel, S., Kohlus, R., & Hinrichs, J. (2018) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2018.11.016 · Cited by 13
High Pressure Processing of Dairy Products
Needs, E. C. (2001) · Food engineering series · doi:10.1007/978-1-4615-0723-9_10 · Cited by 13
Study on zinc ions binding to the individual casein fractions: α-, β- and κ-casein
Rodzik, A., Król‐Górniak, A., Railean‐Plugaru, V., Sugajski, M., Gołębiowski, A., Horne, D. S., Michalke, B., Sprynskyy, M., Pomastowski, P., & Buszewski, B. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.134251 · Cited by 12
Self-citation
Impact of Physicochemical Modifications in Casein Promoted by UV-C on the Peptide Profile of Gastric Digestion and the Transepithelial Transport of Peptides
Morais, A. T. D. B., Morais, S. T. B., Feitor, J. F., Santos, W. G., Catunda, L. G. D. S., Walkling‐Ribeiro, M., Ahrné, L., & Cardoso, D. R. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c00392 · Cited by 12
Influence of Heating Temperature and pH on Acid Gelation of Micellar Calcium Phosphate-Adjusted Skim Milk
Ahmadi, E., Vasiljevic, T., & Huppertz, T. (2024) · Foods · doi:10.3390/foods13111724 · Cited by 12
“MCP stands out as a major factor responsible for maintaining the integrity of the micelle [2,3].”
Background
The Whey Proteins in Milk: Thermal Denaturation, Physical Interactions, and Effects on the Functional Properties of Milk
Anema, S. G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405171-3.00009-x · Cited by 12
Bioavailability and Safety of Food Peptides
de Mejı́a, E. G., Martínez‐Villaluenga, C., Fernández, D., Urado, D., & Sato, K. (2012) · CRC Press eBooks · doi:10.1201/b11768-13 · Cited by 12
Rheological characterization of coffee-flavored yogurt with different types of thickener
Rocha, T. J. O., Mathias, S., de Carvalho, I. C., Wanderlei, C., de Carvalho, P., Flávia, E., & Sérvulo, C. (2011) · Alimentos e Nutrição · Cited by 12
Probing of Competitive Displacement Adsorption of Casein at Oil-in-Water Interface Using Equilibrium Force Distance Measurements
Mahendran, V., Sangeetha, J., & Philip, J. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b02612 · Cited by 12
Use of Surface Plasmon Resonance (SPR) To Study the Dissociation and Polysaccharide Binding of Casein Micelles and Caseins
Thompson, A. K., Singh, H., & Dalgleish, D. G. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf102580r · Cited by 12
Insights into the Interaction of Milk and Dairy Proteins with Aflatoxin M1
Granados-Chinchilla, F. (2016) · InTech eBooks · doi:10.5772/63433 · Cited by 12
Effect of different curd-washing methods on the insoluble Ca content and rheological properties of Colby cheese during ripening
Lee, M.-R., Johnson, M. E., Govindasamy-Lucey, S., Jaeggi, J. J., & Lucey, J. A. (2011) · Journal of Dairy Science · doi:10.3168/jds.2010-3753 · Cited by 11
“Insoluble Ca is a key cross-linking material between CN (Horne, 1998) and a lower INSOL Ca content of cheese can give softer and more meltable cheese (Lucey and Fox, 1993) unless the pH of cheese is very low (pH <4.”
Background
Effect of calcium ions on both the co-assembly of αs-casein with soy phosphatidylcholine and the novel functionality of their complex particles
Semenova, M. G., Anokhina, M. S., Antipova, A. S., Belyakova, L. E., & Polikarpov, Y. N. (2013) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2013.03.018 · Cited by 12
Investigation of surface modification of casein films by rennin enzyme action using micro-beam grazing incidence small angle X-ray scattering
Gebhardt, R., Burghammer, M. C., Riekel, C., Kulozik, U., & Müller‐Buschbaum, P. (2009) · Dairy Science and Technology · doi:10.1051/dst/2009047 · Cited by 12
“micelle models, namely the casein submicelle model [28], the internal structure model [12, 13] and the coat core model [27, 30].”
Method
The Basis of Structure in Dairy-Based Foods: Casein Micelles and their Properties
Dalgleish, D. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404610-8.00003-7 · Cited by 9
Milk Proteins | Casein, Micellar Structure
Horne, D. S. (2011) · Encyclopedia of Dairy Sciences · doi:10.1016/b978-0-12-374407-4.00431-3 · Cited by 12
Self-citation
Comparison of micellar casein isolate and nonfat dry milk for use in the production of high-protein cultured milk products
Wilbanks, D. J., Lee, M. R., Rahimi, Y. S., & Lucey, J. A. (2022) · Journal of Dairy Science · doi:10.3168/jds.2022-22400 · Cited by 10
“These calcium phosphate groups, or colloidal calcium phosphate (CCP), form bridges that crosslink the caseins in the micelle and are solubilized during acidification mainly at pH values 5.0 to 5.5 (Horne, 1998).”
BackgroundInfluential
Proteomic Characterization of Native and Rearranged Disulfide Bonds in Proteins from Thermally Treated and Commercial Milk Samples
Ciaravolo, V., Scaloni, A., Novi, G., Renzone, G., & Arena, S. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c01689 · Cited by 11
Immobilization of silver ions onto casein
Dyrda-Terniuk, T., Pryshchepa, O., Rafińska, K., Kolankowski, M., Gołębiowski, A., Gloc, M., Dobrucka, R., Kurzydłowski, K. J., & Pomastowski, P. (2023) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2023.131390 · Cited by 11
The structural changes of a bovine casein micelle during temperature change; in situ observation over a wide spatial scale from nano to micrometer
Takagi, H., Nakano, T., Aoki, T., & Tanimoto, M. (2023) · Soft Matter · doi:10.1039/d3sm00146f · Cited by 11
Cheese | Rennet-Induced Coagulation of Milk
Gregersen, V., & Lucey, J. (2011) · Elsevier eBooks · doi:10.1016/b978-0-08-100596-5.00684-3 · Cited by 18
Inherent and process-induced hydrophobicity influences aroma retention in fat-free dairy matrices
Heilig, A., Çetin, S., Erpenbach, K., Höhn, J., & Hinrichs, J. (2011) · International Dairy Journal · doi:10.1016/j.idairyj.2011.01.002 · Cited by 11
Rheology of Swiss Cheese Fondue
Bertsch, P., Savorani, L., & Fischer, P. (2019) · ACS Omega · doi:10.1021/acsomega.8b02424 · Cited by 12
Milk
Eskin, N. A. M., & Goff, H. D. (2012) · Elsevier eBooks · doi:10.1016/b978-0-08-091809-9.00004-2 · Cited by 11
Casein Microparticles from Blend Films Forming Casein/α-Tocopherol Emulsion Droplets in Solution
Zhuang, Y., Sterr, J., Schulte, A., Kulozik, U., & Gebhardt, R. (2016) · Food Biophysics · doi:10.1007/s11483-016-9446-3 · Cited by 11
From Micelle to Melt: The Influence of Calcium on Physico‐chemical Properties of Cheese
Cooke, D. R., & McSweeney, P. L. H. (2017) · Wiley eBooks · doi:10.1002/9781119046165.ch0b · Cited by 11
Protein-Protein Interactions in Food
Corredig, M. (2005) · Food science and technology · doi:10.1201/9781420028133.ch8 · Cited by 10
Re-association Behavior of Casein Submicelles in Highly Alkaline Environments
Bian, H., & Plank, J. (2012) · Zeitschrift für Naturforschung B · doi:10.5560/znb.2012-0035 · Cited by 10
Heat-Induced Casein–Whey Protein Interactions
Gunasekaran, S., & Solar, O. (2012) · CRC Press eBooks · doi:10.1201/b11768-9 · Cited by 10
Use of water-soluble soy extract and inulin as ingredients to produce a fermented dairy beverage made from caprine milk
Ribeiro, J. E. S., Sant’Ana, A. M. D. S., da Silva, F. L. H., & Filho, E. M. B. (2022) · Food Science and Technology · doi:10.1590/fst.102122 · Cited by 10
Microfiltration of concentrated milk protein dispersions: The role of pH and minerals on the performance of silicon nitride microsieves
Carpintero‐Tepole, V., la Fuente, E. B., Martínez-González, E., & Torrestiana‐Sanchez, B. (2014) · LWT · doi:10.1016/j.lwt.2014.06.057 · Cited by 10
“Otherwise, casein micelle structure is maintained by colloidal calcium phosphate (CCP), attractive hydrophobic interactions and repulsive electrostatic or electrical double layer forces (Horne, 1998).”
Background
Post-translational modifications of caseins
Holland, J. W. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-374039-7.00004-0 · Cited by 10
Chapter VI Caseins
de Kruif, C. G. (2003) · Progress in biotechnology · doi:10.1016/s0921-0423(03)80006-0 · Cited by 10
Behaviour of partially cross‐linked casein micelles under high pressure
Huppertz, T., & Smiddy, M. A. (2008) · International Journal of Dairy Technology · doi:10.1111/j.1471-0307.2008.00370.x · Cited by 10
Effect of sodium chloride addition during diafiltration on the solubility of milk protein concentrate
Gualco, S. J. (2010) · doi:10.15368/theses.2010.190 · Cited by 10
“95 Although no significant differences in Ca content were found in this particular study, this data is generally consistent with what has been previously reported concerning the effect of mineral addition on the Ca system in milk (Dalgleish and Parker, 1980, Dickson and Perkins, 1971, Horne, 1998).”
BackgroundResultInfluential
Designing tailor-made steric matters to improve the immobilized ficin specificity for small versus large proteins
Siar, E.-H., Abellanas-Pérez, P., Morellon‐Sterling, R., Bolivar, J. M., Rocha‐Martín, J., & Fernández‐Lafuente, R. (2024) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2024.09.005 · Cited by 9
The enzyme-mediated autodeposition of casein: effect of enzyme immobilization on deposition of protein structures
Ruediger, A. A., Bremser, W., & Strube, O. I. (2016) · Journal of Coatings Technology and Research · doi:10.1007/s11998-015-9757-1 · Cited by 9
Effects of Pulsed Electric Fields on Food Constituents, Microstructure and Sensorial Attributes of Food Products
Yang, S., Liu, G., Qin, Z., Munk, D. M. E., Otte, J., & Ahrné, L. (2019) · Springer eBooks · doi:10.1007/978-3-030-18191-8_2 · Cited by 9
Acidification of lactoferrin-casein micelle complexes in skim milk
Anema, S. G. (2019) · International Dairy Journal · doi:10.1016/j.idairyj.2019.104550 · Cited by 9

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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks