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 201–300 of 727

Celecoxib Encapsulation in β-Casein Micelles: Structure, Interactions, and Conformation
Turovsky, T., Khalfin, R. L., Kababya, S., Schmidt, A., Barenholz, Y., & Danino, D. (2015) · Langmuir · doi:10.1021/acs.langmuir.5b01397 · Cited by 49
Exopolysaccharide production by three different strains of S treptococcus thermophilus and its effect on physical properties of acidified milk
Mende, S., Mentner, C., Thomas, S., Rohm, H., & Jaros, D. (2012) · Engineering in Life Sciences · doi:10.1002/elsc.201100114 · Cited by 48
Effect of increasing the colloidal calcium phosphate of milk on the texture and microstructure of yogurt
Özcan, T., Horne, D. S., & Lucey, J. A. (2011) · Journal of Dairy Science · doi:10.3168/jds.2010-3932 · Cited by 48
Self-citation
How to tailor heat-induced whey protein/κ-casein complexes as a means to investigate the acid gelation of milk—a review
Morand, M., Guyomarc’H, F., & Famelart, M. (2011) · Dairy Science and Technology · doi:10.1007/s13594-011-0013-x · Cited by 48
Improving Clarity and Stability of Skim Milk Powder Dispersions by Dissociation of Casein Micelles at pH 11.0 and Acidification with Citric Acid
Pan, K., & Zhong, Q. (2013) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf402870y · Cited by 48
Pressure-induced dissociation of casein micelles: size distribution and effect of temperature
Gebhardt, R., Doster, W., & Kulozik, U. (2005) · Brazilian Journal of Medical and Biological Research · doi:10.1590/s0100-879x2005000800008 · Cited by 48
Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics
Markoska, T., Daniloski, D., Vasiljevic, T., & Huppertz, T. (2021) · Molecules · doi:10.3390/molecules26247650 · Cited by 47
Effect of milk solids concentration on the gels formed by the acidification of heated pH-adjusted skim milk
Anema, S. G. (2007) · Food Chemistry · doi:10.1016/j.foodchem.2007.10.051 · Cited by 47
Optimization of the prebiotic & probiotic concentration and incubation temperature for the preparation of synbiotic soy yoghurt using response surface methodology
Pandey, S. M., & Mishra, H. N. (2014) · LWT · doi:10.1016/j.lwt.2014.12.003 · Cited by 47
Ethanol Stability and Milk Composition
Horne, D. S. (2015) · Springer eBooks · doi:10.1007/978-1-4939-2800-2_9 · Cited by 47
Self-citation
Self-association of bovine β-casein as influenced by calcium chloride, buffer type and temperature
Li, M., Auty, M. A. E., Crowley, S. V., Kelly, A. L., O’Mahony, J. A., & Brodkorb, A. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.09.035 · Cited by 47
Functional and dysfunctional folding, association and aggregation of caseins
Carver, J. A., & Holt, C. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.09.002 · Cited by 47
Formation, Structural Properties and Rheology of Acid-coagulated Milk Gels
Lucey, J. A. (2004) · Cheese · doi:10.1016/s1874-558x(04)80064-2 · Cited by 48
Ultrasonic shear wave rheology of weak particle gels
Buckin, V. A., & Kudryashov, E. (2001) · Advances in Colloid and Interface Science · doi:10.1016/s0001-8686(00)00060-9 · Cited by 47
Binding of vitamin A by casein micelles in commercial skim milk
Mohan, M. S., Jurat‐Fuentes, J. L., & Harte, F. (2012) · Journal of Dairy Science · doi:10.3168/jds.2012-5777 · Cited by 46
The effect of free Ca2+ on the heat stability and other characteristics of low-heat skim milk powder
Faka, M., Lewis, M. J., Grandison, A. S., & Deeth, H. C. (2009) · International Dairy Journal · doi:10.1016/j.idairyj.2008.12.006 · Cited by 46
Experimental evidence for previously unclassified calcium phosphate structures in the casein micelle
Hindmarsh, J. P., & Watkinson, P. J. (2017) · Journal of Dairy Science · doi:10.3168/jds.2017-12623 · Cited by 47
Optimization of the Electrodeposition of Gold Nanoparticles for the Application of Highly Sensitive, Label-Free Biosensor
Chiang, H.-C., Wang, Y.-Y., Zhang, Q., & Levon, K. (2019) · Biosensors · doi:10.3390/bios9020050 · Cited by 48
Decoupling Macronutrient Interactions during Heating of Model Infant Milk Formulas
Murphy, E. G., Fenelon, M. A., Roos, Y. H., & Hogan, S. A. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf503620r · Cited by 45
Effects of processing conditions on the texture and rheological properties of model acid gels and cream cheese
Brighenti, M., Govindasamy-Lucey, S., Jaeggi, J. J., Johnson, M. E., & Lucey, J. A. (2018) · Journal of Dairy Science · doi:10.3168/jds.2018-14391 · Cited by 49
A perspective on the characterization of colloids and macromolecules using asymmetrical flow field-flow fractionation
Runyon, J. R., Ulmius, M., & Nilsson, L. (2013) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2013.04.010 · Cited by 45
Aggregation and gelation of micellar casein particles
Panouillé, M., Durand, D., Nicolaï, T., Larquet, É., & Boisset, N. (2005) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2005.02.008 · Cited by 45
Impact of Casein Gel Microstructure on Self-Diffusion Coefficient of Molecular Probes Measured by 1H PFG-NMR
Feunteun, S. L., & Mariette, F. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf071982v · Cited by 45
Functionality of Ingredients: Emulsifying Salts
Lucey, J. A., Maurer‐Rothmann, A., & Kaliappan, S. (2011) · Wiley eBooks · doi:10.1002/9781444341850.ch4 · Cited by 45
Reassembling of Alkali-Treated Casein Micelles by Microbial Transglutaminase
Duerasch, A., Wissel, J., & Henle, T. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b04000 · Cited by 44
Fully recycling dairy wastewater by an integrated isoelectric precipitation–nanofiltration–anaerobic fermentation process
Chen, Z., Luo, J., Chen, X., Hang, X., Shen, F., & Wan, Y. (2015) · Chemical Engineering Journal · doi:10.1016/j.cej.2015.07.086 · Cited by 44
Casein, Caseinates, and Milk Protein Concentrates
Augustin, M. A., Oliver, C. M., & Hémar, Y. (2011) · doi:10.1002/9780470959169.ch7 · Cited by 44
Avaliação do comportamento reológico de diferentes iogurtes comerciais
Mathias, T. R. D. S., Andrade, K. C. S., Rosa, C. L. D. S., & Silva, B. A. (2013) · Brazilian journal of food technology/Brazilian Journal of Food Technology · doi:10.1590/s1981-67232013005000004 · Cited by 43
Use of sodium polyphosphates with different linear lengths in the production of spreadable processed cheese
Nagyová, G., Buňka, F., Salek, R. N., Černíková, M., Mančík, P., Grůber, T., & Kuchař, D. (2013) · Journal of Dairy Science · doi:10.3168/jds.2013-7210 · Cited by 43
Proteomic Quantification of Disulfide-Linked Polymers in Raw and Heated Bovine Milk
Chevalier, F., & Kelly, A. L. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf1010879 · Cited by 43
Some perspectives on the use of cheese as a food ingredient
Lucey, J. A. (2008) · Dairy Science and Technology · doi:10.1051/dst:2008010 · Cited by 44
Syneresis investigations of lacto-fermented sodium caseinate in a mixed model system
Bouchikhi, S. E., Pagès, P., Alaoui, Y. E., Ibrahimi, A., & Bensouda, Y. (2019) · BMC Biotechnology · doi:10.1186/s12896-019-0539-1 · Cited by 43
Posttranslational modifications of caseins
Bijl, E., Holland, J. W., & Boland, M. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815251-5.00005-0 · Cited by 45
Light scattering study of sodium caseinate+dextran sulfate in aqueous solution: Relationship to emulsion stability
Semenova, M. G., Belyakova, L. E., Polikarpov, Y. N., Antipova, A. S., & Dickinson, E. (2008) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2008.06.010 · Cited by 43
Milk protein gels
Lucey, J. (2020) · Milk Proteins · doi:10.1016/b978-0-12-374039-7.00016-7 · Cited by 49
Modifications of the charges at the N-terminus of bovine β-casein: Consequences on its structure and its micellisation
Gangnard, S., Zuev, Y. F., Gaudin, J., Fedotov, V. D., Choiset, Y., Axelos, M., Chobert, J., & Haertlé, T. (2006) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2006.03.007 · Cited by 42
Application of Response Surface Methodology to Improve Fermentation Time and Rheological Properties of Probiotic Yogurt Containing Lactobacillus reuteri
Bitaraf, M. S., Khodaiyan, F., Mohammadifar, M. A., & Mousavi, S. M. (2010) · Food and Bioprocess Technology · doi:10.1007/s11947-010-0433-2 · Cited by 42
Factors influencing the gelation and rennetability of camel milk using camel chymosin
Hailu, Y., Hansen, E. B., Seifu, E., Eshetu, M., & Ipsen, R. (2016) · International Dairy Journal · doi:10.1016/j.idairyj.2016.01.013 · Cited by 42
Microparticulated whey protein addition modulates rheological and microstructural properties of high-protein acid milk gels
Silva, J. V. C., & O’Mahony, J. A. (2017) · International Dairy Journal · doi:10.1016/j.idairyj.2017.11.013 · Cited by 42
Interactions of Casein and Polypeptides in Multilayer Films Studied by FTIR and Molecular Dynamics
Szyk‐Warszyńska, L., Raszka, K., & Warszyński, P. (2019) · Polymers · doi:10.3390/polym11050920 · Cited by 42
Effect of Sodium Bisulfite on Properties of Soybean Glycinin
Zhang, L., & Sun, X. S. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf801137y · Cited by 41
Different coagulation behaviour of bacteriologically acidified and renneted milk: the importance of fine-tuning acid production and rennet action
Tranchant, C. C., Dalgleish, D. G., & Hill, A. R. (2001) · International Dairy Journal · doi:10.1016/s0958-6946(01)00069-3 · Cited by 41
Simulating the self-association of caseins
Euston, S. R., & Horne, D. S. (2004) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2004.10.004 · Cited by 40
Self-citation
The interaction, stability and response to an external stimulus of iron oxide nanoparticle–casein nanocomplexes
Sangeetha, J., & Philip, J. (2012) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2012.04.049 · Cited by 40
Mixed protein–surfactant adsorption layers formed in a sequential and simultaneous way at water–air and water–oil interfaces
Dan, A., Kotsmar, C., Ferri, J. K., Javadi, A., Karbaschi, M., Krägel, J., Wüstneck, R., & Miller, R. (2012) · Soft Matter · doi:10.1039/c2sm25463h · Cited by 39
Avaliação físico-química, microbiológica e reológica de bebida láctea e leite fermentado adicionados de probióticos
Cunha, T. M., de Castro, F. P., Barreto, P. L. M., Benedet, H. D., & Prudêncio, E. S. (2008) · Semina Ciências Agrárias · doi:10.5433/1679-0359.2008v29n1p103 · Cited by 38
Spatial arrangement of casein micelles and whey protein aggregate in acid gels: Insight on mechanisms
Andoyo, R., Guyomarc’H, F., Burel, A., & Famelart, M. (2015) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2015.04.031 · Cited by 39
Determination of molecular weight of a purified fraction of colloidal calcium phosphate derived from the casein micelles of bovine milk
Choi, J.-W., Horne, D. S., & Lucey, J. A. (2011) · Journal of Dairy Science · doi:10.3168/jds.2010-3762 · Cited by 38
Self-citation
Contributions of Terminal Peptides to the Associative Behavior of αs1-Casein
Malin, E. L., Brown, E. M., Wickham, E. D., & Farrell, H. M. (2005) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(05)72910-6 · Cited by 38
Molecular Mechanism of the Renneting Process of Casein Micelles in Skim Milk, Examined by Viscosity and Light-Scattering Experiments and Simulated by Model SCF Calculations
Mellema, M., Leermakers, F. A. M., & de Kruif, C. G. (1999) · Langmuir · doi:10.1021/la9902340 · Cited by 38
Ethanol Stability
Horne, D. S. (2003) · Springer eBooks · doi:10.1007/978-1-4419-8602-3_27 · Cited by 38
Self-citation
What is the impact of amino acid mutations in the primary structure of caseins on the composition and functionality of milk and dairy products?
Daniloski, D., McCarthy, N., Huppertz, T., & Vasiljevic, T. (2022) · Current Research in Food Science · doi:10.1016/j.crfs.2022.09.026 · Cited by 33
Effects of enzyme-induced carbonate precipitation technique on multiple heavy metals immobilization and unconfined compressive strength improvement of contaminated sand
Yi, B., Chen, Y., Zhan, L., Guo, H., Ke, H., Wang, Y., Wang, Q., Gao, Y., & Gao, Y. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.174409 · Cited by 39
The association of low-molecular-weight hydrophobic compounds with native casein micelles in bovine milk
Cheema, M. K., Mohan, M. S., Campagna, S. R., Jurat‐Fuentes, J. L., & Harte, F. (2015) · Journal of Dairy Science · doi:10.3168/jds.2015-9461 · Cited by 37
Effects of sodium chloride salting and substitution with potassium chloride on whey expulsion of Cheddar cheese
Lu, Y., & McMahon, D. J. (2014) · Journal of Dairy Science · doi:10.3168/jds.2014-8600 · Cited by 40
Changes in the calcium cluster distribution of ultrafiltered and diafiltered fresh skim milk as observed by Small Angle Neutron Scattering
Alexander, M., Nieh, M., Ferrer, M. A., & Corredig, M. (2011) · Journal of Dairy Research · doi:10.1017/s0022029911000409 · Cited by 37
Sequence characteristics responsible for protein‐protein interactions in the intrinsically disordered regions of caseins, amelogenins, and small heat‐shock proteins
Holt, C., Raynes, J. K., & Carver, J. A. (2019) · Biopolymers · doi:10.1002/bip.23319 · Cited by 37
Chromosomal Regions Underlying Noncoagulation of Milk in Finnish Ayrshire Cows
Tyrisevä, A.-M., Elo, K., Kuusipuro, A., Vilva, V., Jänönen, I., Karjalainen, H., Ikonen, T., & Ojala, M. (2008) · Genetics · doi:10.1534/genetics.107.083964 · Cited by 36
Rennet-induced coagulation properties of yak casein micelles: A comparison with cow casein micelles
Zhang, Y., Li, Y., Wang, P., Tian, Y., Liang, Q., & Ren, F. (2017) · Food Research International · doi:10.1016/j.foodres.2017.09.097 · Cited by 36
Interfacial properties of acidified skim milk
Cases, E., Rampini, C., & Cayot, P. (2004) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2004.08.115 · Cited by 36
Unfolding and refolding details of lysozyme in the presence of β-casein micelles
Wu, F., Luo, J., & Yu, Z. (2011) · Physical Chemistry Chemical Physics · doi:10.1039/c0cp01184c · Cited by 36
Small and Large Deformation Rheology of Acid Gels from Transglutaminase Treated Milks
Jaros, D., Pätzold, J., Schwarzenbolz, U., & Rohm, H. (2006) · Food Biophysics · doi:10.1007/s11483-006-9016-1 · Cited by 36
Structural Changes of Casein Micelles in a Calcium Gradient Film
Gebhardt, R., Burghammer, M. C., Riekel, C., Roth, S. V., & Müller‐Buschbaum, P. (2007) · Macromolecular Bioscience · doi:10.1002/mabi.200700203 · Cited by 36
Rheological Properties of Rennet Gels Containing Milk Protein Concentrates
Ferrer, M. A., Hill, A. R., & Corredig, M. (2008) · Journal of Dairy Science · doi:10.3168/jds.2007-0525 · Cited by 36
Effects of the Concentration of Insoluble Calcium Phosphate Associated with Casein Micelles on the Functionality of Directly Acidified Cheese
Choi, J.-W., Horne, D. S., Johnson, M. E., & Lucey, J. A. (2008) · Journal of Dairy Science · doi:10.3168/jds.2007-0454 · Cited by 36
Self-citation
EFFECT OF TEMPERATURE AND RATE OF ACIDIFICATION ON THE RHEOLOGICAL PROPERTIES OF ACID SKIM MILK GELS
Anema, S. G. (2008) · Journal of Food Processing and Preservation · doi:10.1111/j.1745-4549.2008.00230.x · Cited by 35
Segregative interactions and competitive binding of Ca2+ in gelling mixtures of whey protein isolate with Na+ κ-carrageenan
Harrington, J. C., Foegeding, E. A., Mulvihill, D. M., & Morris, E. R. (2008) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2008.03.007 · Cited by 35
Mozzarella Cheese – A Review of the Structural Development During Processing
Smith, J. R., Carr, A. J., Golding, M., & Reid, D. S. (2017) · Food Biophysics · doi:10.1007/s11483-017-9511-6 · Cited by 36
Nutritional Quality, Sensory Analysis and Shelf Life Stability of Yogurts Containing Inulin-Type Fructans and Winery Byproducts for Sustainable Health
Iriondo-DeHond, M., Blázquez-Duff, J. M., del Castillo, M. D., & Miguel, E. (2020) · Foods · doi:10.3390/foods9091199 · Cited by 37
Nano-scale core–shell structural casein based coating latex: Synthesis, characterization and its biodegradability
Ma, J., Xu, Q., Zhou, J., Gao, D., Zhang, J., & Chen, L. (2013) · Progress in Organic Coatings · doi:10.1016/j.porgcoat.2013.04.006 · Cited by 35
αS1-casein, which is essential for efficient ER-to-Golgi casein transport, is also present in a tightly membrane-associated form
Parc, A. L., Léonil, J., & Chanat, E. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-65 · Cited by 35
Association of Triclosan to Casein Proteins Through Solvent‐Mediated High‐Pressure Homogenization
Roach, A., Dunlap, J., & Harte, F. (2009) · Journal of Food Science · doi:10.1111/j.1750-3841.2009.01048.x · Cited by 35
Influence of calcium-binding salts on heat stability and fouling of whey protein isolate dispersions
Hebishy, E., Joubran, Y., Murphy, E. G., & O’Mahony, J. A. (2018) · International Dairy Journal · doi:10.1016/j.idairyj.2018.12.003 · Cited by 34
Study on internal structure of casein micelles in reconstituted skim milk powder
Du, Z., Xu, N., Yang, Y., Li, G., Tai, Z., Li, N., & Sun, Y. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.10.135 · Cited by 34
Equilibrium and dynamics of adsorption of mixed β-casein/surfactant solutions at the water/hexane interface
Kotsmár, C., Aksenenko, E. V., Fainerman, V. B., Pradines, V., Krägel, J., & Miller, R. (2009) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2009.04.025 · Cited by 34
Use of time–temperature superposition to study the rheological properties of cheese during heating and cooling
Udyarajan, C. T., Horne, D. S., & Lucey, J. A. (2007) · International Journal of Food Science & Technology · doi:10.1111/j.1365-2621.2006.01468.x · Cited by 34
Self-citation
The Quality of Milk for Cheese Manufacture
Guinee, T. P., & O’Brien, B. (2010) · Wiley eBooks · doi:10.1002/9781444323740.ch1 · Cited by 36
Reducing the level of added disodium phosphate alters the chemical and physical properties of processed cheese
Guinee, T. P., & O’Kennedy, B. T. (2012) · Dairy Science and Technology · doi:10.1007/s13594-011-0053-2 · Cited by 33
Addition of calcium and magnesium chlorides as simple means of varying bound and precipitated minerals in casein micelle: Effect on enzymatic coagulation
Bauland, J., Famelart, M., Bouhallab, S., Jeantet, R., ROUSTEL, S., FAIVELEY, M., & Croguennec, T. (2020) · Journal of Dairy Science · doi:10.3168/jds.2020-18749 · Cited by 33
Use of casein micelles to improve the solubility of hydrophobic pea proteins in aqueous solutions via low-temperature homogenization
Krentz, A., García‐Cano, I., Ortega‐Anaya, J., & Jiménez‐Flores, R. (2021) · Journal of Dairy Science · doi:10.3168/jds.2021-20902 · Cited by 33
New Insights into Cheese Microstructure
Ong, L., Li, X., Ong, A., & Gras, S. L. (2022) · Annual Review of Food Science and Technology · doi:10.1146/annurev-food-032519-051812 · Cited by 35
Partial replacement of β-casein by napin, a rapeseed protein, as ingredient for processed foods: Thermoreversible aggregation
Schwartz, J.-M., Solé-Jamault, V., Guéguen, J., Ropers, M., Riaublanc, A., & Anton, M. (2015) · LWT · doi:10.1016/j.lwt.2015.03.084 · Cited by 33
Disulphide bonds in casein micelle from milk
Bouguyon, E., Beauvallet, C., Huet, J., & Chanat, E. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.005 · Cited by 33
Chymosin, Pepsins and Other Aspartyl Proteinases: Structures, Functions, Catalytic Mechanism and Milk-Clotting Properties
Uniacke‐Lowe, T., & Fox, P. F. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-417012-4.00004-1 · Cited by 36
Fermented whey beverages: A review of process fundamentals, recent developments and nutritional potential
Bandara, T., Munasinghe-Arachchige, S. P., & Gamlath, C. J. (2023) · International Journal of Dairy Technology · doi:10.1111/1471-0307.12993 · Cited by 28
The effect of emulsifying salts on the turbidity of a diluted milk system with varying pH and protein concentration
Culler, M. D., Sariçay, Y., & Harte, F. (2017) · Journal of Dairy Science · doi:10.3168/jds.2017-12549 · Cited by 32
Nanoparticles of casein micelles for encapsulation of food ingredients
Chen, H., Wooten, H., Thompson, L., & Pan, K. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-815663-6.00002-1 · Cited by 32
Structural changes of deposited casein micelles induced by membrane filtration
Gebhardt, R., Steinhauer, T., Meyer, P., Sterr, J., Perlich, J., & Kulozik, U. (2012) · Faraday Discussions · doi:10.1039/c2fd20022h · Cited by 32
Camel and Bovine Chymosin Hydrolysis of Bovine α S1 - and β-Caseins Studied by Comparative Peptide Mapping
Møller, K. K., Rattray, F. P., & Ardö, Y. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf302890h · Cited by 32
Spontaneous interaction of lactoferrin with casein micelles or individual caseins
Anema, S. G. (2018) · Journal of the Royal Society of New Zealand · doi:10.1080/03036758.2018.1439846 · Cited by 32
Effect of exopolysaccharide-producing Lactococcus lactis strains and temperature on the permeability of skim milk gels.
Ruas‐Madiedo, P., & Zoon, P. (2003) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/s0927-7757(02)00517-4 · Cited by 32
Modelling casein aggregation and curd firming in goats' milk from backscatter of infrared light.
Castillo, M., Payne, F., Hicks, C. L., Laencina, J., & López, M.-B. (2003) · Journal of Dairy Research · doi:10.1017/s0022029903006356 · Cited by 31
Influence of citrate- and phosphate-based calcium sequestering salts on the disruption of casein micelles
Deshwal, G. K., Fenelon, M. A., Gómez‐Mascaraque, L. G., & Huppertz, T. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.109970 · Cited by 31
Influence of dispersed particles on small and large deformation properties of concentrated caseinate composites
Manski, J. M., Kretzers, I. M. J., van Brenk, S., van der Goot, A. J., & Boom, R. M. (2006) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2006.02.002 · Cited by 31
Acoustic characterisation of pH dependant reversible micellar casein aggregation
Francis, M. J., Glover, Z. J., Yu, Q., Povey, M., & Holmes, M. J. (2019) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2019.02.026 · Cited by 30
Physicochemical properties of skim milk powder dispersions prepared with calcium-chelating sodium tripolyphosphate, trisodium citrate, and sodium hexametaphosphate
Choi, I., & Zhong, Q. (2020) · Journal of Dairy Science · doi:10.3168/jds.2020-18644 · Cited by 30
The whey proteins in milk: Thermal denaturation, physical interactions, and effects on the functional properties of milk
Anema, S. G. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815251-5.00009-8 · Cited by 30
Physicochemical Variables Affecting the Rheology and Microstructure of Rennet Casein Gels
Zhong, Q., Daubert, C. R., & Velev, O. D. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0625914 · Cited by 30
Cryo-SEM images of native milk fat globule indicate small casein micelles are constituents of the membrane
Luo, J., Wang, Z. W., Wang, F., Zhang, H., Lu, J., Guo, H., & Ren, F. (2014) · RSC Advances · doi:10.1039/c4ra06171c · Cited by 30
Peptidomic screening of bitter and nonbitter casein hydrolysate fractions for insulinogenic peptides
Murray, N. M., O’Riordan, D., Jacquier, J., O’Sullivan, M., Holton, T. A., Wynne, K. J., Robinson, R. C., Barile, D., Nielsen, S. D.-H., & Dallas, D. C. (2018) · Journal of Dairy Science · doi:10.3168/jds.2017-13853 · Cited by 29

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