Cited by 347Proteins in Food SystemsProtein Hydrolysis and Bioactive PeptidesMicroencapsulation and Drying Processes

The DOI matches its Crossref record; 244 of the 244 references it cites were found in a registry or an index.

Modifications of structures and functions of caseins: a scientific and technological challenge.

Open access

Broyard, Camille, Gaucheron, Frédéric·2015·Dairy Science & Technology

DOI 10.1007/s13594-015-0220-y

Open this paper in CoChat — free account Open PDF

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1007/s13594-015-0220-y

Cites

244 of 244 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Dairy Science and Technology
Walstra, P., Walstra, P., Wouters, J. T. M., & Geurts, T. J. (2005) · doi:10.1201/9781420028010 · Cited by 1,788
Dairy Chemistry and Biochemistry
Fox, P. F., Uniacke‐Lowe, T., McSweeney, P. L. H., & O’Mahony, J. A. (2015) · Springer eBooks · doi:10.1007/978-3-319-14892-2 · Cited by 1,647
Physical Chemistry of Foods
Walstra, P. (2002) · CRC Press eBooks · doi:10.1201/9780203910436 · Cited by 1,054
Milk proteins as vehicles for bioactives
Livney, Y. D. (2009) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2009.11.002 · Cited by 948
The Structure of the Casein Micelle of Milk and Its Changes During Processing
Dalgleish, D. G., & Corredig, M. (2012) · Annual Review of Food Science and Technology · doi:10.1146/annurev-food-022811-101214 · Cited by 651
The minerals of milk
Gaucheron, F. (2005) · annales de biologie animale biochimie biophysique · doi:10.1051/rnd:2005030 · Cited by 620
Self-citation
Effect of heating on Maillard reactions in milk
van Boekel, M. A. J. S. (1998) · Food Chemistry · doi:10.1016/s0308-8146(98)00075-2 · Cited by 578
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 micelles and their internal structure
de Kruif, C. G., Huppertz, T., Urban, V. S., et al. (2012) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2012.01.002 · Cited by 542
Enhancing the functionality of food proteins by enzymatic modification
Panyam, D., & Kilara, A. (1996) · Trends in Food Science & Technology · doi:10.1016/0924-2244(96)10012-1 · Cited by 528
Invited review: Caseins and the casein micelle: Their biological functions, structures, and behavior in foods
Holt, C., Carver, J. A., Ecroyd, H. W., & Thorn, D. C. (2013) · Journal of Dairy Science · doi:10.3168/jds.2013-6831 · Cited by 516
On the structural models of bovine casein micelles—review and possible improvements
Dalgleish, D. G. (2010) · Soft Matter · doi:10.1039/c0sm00806k · Cited by 503
Structure and Stability of Bovine Casein Micelles
Holt, C. (1992) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60554-9 · Cited by 487
Food protein functionality: A comprehensive approach
Foegeding, E. A., & Davis, J. P. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.05.008 · Cited by 486
Methyl‐CpG‐binding proteins
Ballestar, E., & Wolffe, A. P. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.01869.x · Cited by 413
Significance and applications of phenolic compounds in the production and quality of milk and dairy products: a review
O'Connell, J. E. A., & Fox, P. F. (2001) · International Dairy Journal · doi:10.1016/s0958-6946(01)00033-4 · Cited by 410
Glycation a promising method for food protein modification: Physicochemical properties and structure, a review
Liu, J., Ru, Q., & Ding, Y. (2012) · Food Research International · doi:10.1016/j.foodres.2012.07.034 · Cited by 396
Chemistry of the Caseins
Swaisgood, H. E. (2003) · Springer eBooks · doi:10.1007/978-1-4419-8602-3_3 · Cited by 390
The casein micelle: Historical aspects, current concepts and significance
Fox, P. F., & Brodkorb, A. (2008) · International Dairy Journal · doi:10.1016/j.idairyj.2008.03.002 · Cited by 390
Casein Micelle Structure, Functions and Interactions
de Kruif, C. G., & Holt, C. (2003) · Springer eBooks · doi:10.1007/978-1-4419-8602-3_5 · Cited by 367
Physicochemical characterization of Remsima®
Jung, S. K., Lee, K. H., Jeon, J. W., Lee, J. W., Kwon, B., Kim, Y. J., Bae, J. S., Kim, D., Lee, S. Y., & Chang, S.-J. (2014) · mAbs · doi:10.4161/mabs.32221 · Cited by 352
Casein sub-micelles: do they exist?
Walstra, P. (1999) · International Dairy Journal · doi:10.1016/s0958-6946(99)00059-x · Cited by 343
Transglutaminase Catalyzed Reactions: Impact on Food Applications
DeJong, G. A. H., & Koppelman, S. J. (2002) · Journal of Food Science · doi:10.1111/j.1365-2621.2002.tb08819.x · Cited by 337
Effect of heat treatment on milk protein functionality at emulsion interfaces. A review
Raikos, V. (2009) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2009.10.014 · Cited by 315
Heat-Induced Changes in Milk
Fox, P. F., Uniacke‐Lowe, T., McSweeney, P. L. H., & O’Mahony, J. A. (2015) · Springer eBooks · doi:10.1007/978-3-319-14892-2_9 · Cited by 297
Solubility and emulsifying properties of caseins and whey proteins modified enzymically by trypsin
Chobert, J. M., Bertrand-Harb, C., & Nicolas, M. G. (1988) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00083a002 · Cited by 296
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
Formation and properties of the whey protein/κ-casein complexes in heated skim milk – A review
Donato, L., & Guyomarc’H, F. (2009) · Dairy Science and Technology · doi:10.1051/dst:2008033 · Cited by 293
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
Stability of casein micelles in milk
Tuinier, R., & de Kruif, C. G. (2002) · The Journal of Chemical Physics · doi:10.1063/1.1484379 · Cited by 269
Effect of pH on the Association of Denatured Whey Proteins with Casein Micelles in Heated Reconstituted Skim Milk
Anema, S. G., & Li, Y. (2003) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf025673a · Cited by 260
A possible structure of the casein micelle based on high-resolution field-emission scanning electron microscopy
Dalgleish, D. G., Spagnuolo, P. A., & Goff, H. D. (2004) · International Dairy Journal · doi:10.1016/j.idairyj.2004.04.008 · Cited by 251
Association of caseins and casein micelle structure.
Schmidt, D. G. (1982) · Cited by 246
High pressure treatment of bovine milk: effects on casein micelles and whey proteins
Huppertz, T., Fox, P. F., & Kelly, A. L. (2004) · Journal of Dairy Research · doi:10.1017/s002202990300640x · Cited by 243
Effects of the environmental factors on the casein micelle structure studied by cryo transmission electron microscopy and small-angle x-ray scattering/ultrasmall-angle x-ray scattering
Marchin, S., Putaux, J., Pignon, F., & Léonil, J. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2409933 · Cited by 242
Effects of Enzymatic Deamidation by Protein-Glutaminase on Structure and Functional Properties of Wheat Gluten
Yong, Y. H., Yamaguchi, S., & Matsumura, Y. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf060344u · Cited by 236
How to Squeeze a Sponge: Casein Micelles under Osmotic Stress, a SAXS Study
Bouchoux, A., Gésan-Guiziou, G., Pérez, J., et al. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.10.019 · Cited by 220
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
TRANSGLUTAMINASE IN DAIRY PRODUCTS: CHEMISTRY, PHYSICS, APPLICATIONS
Jaros, D., Partschefeld, C., Henle, T., et al. (2006) · Journal of Texture Studies · doi:10.1111/j.1745-4603.2006.00042.x · Cited by 210
Genipin-crosslinked casein hydrogels for controlled drug delivery
Song, F., Zhang, L., Yang, C. H., & Li, Y. (2009) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2009.02.005 · Cited by 185
Incorporation of microbial transglutaminase into non-fat yogurt production
Özer, B., Kırmacı, H. A., Öztekin, Ş., et al. (2006) · International Dairy Journal · doi:10.1016/j.idairyj.2006.02.007 · Cited by 180
Structure formation in casein-based gels, foams, and emulsions
Dickinson, E. (2006) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2006.01.012 · Cited by 173
Effects of Emulsifying Salts on the Turbidity and Calcium-Phosphate–Protein Interactions in Casein Micelles
Mizuno, R., & Lucey, J. A. (2005) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(05)72988-x · Cited by 171
A Novel Protein-Deamidating Enzyme from Chryseobacterium proteolyticum sp. nov., a Newly Isolated Bacterium from Soil
Yamaguchi, S., & Yokoe, M. (2000) · Applied and Environmental Microbiology · doi:10.1128/aem.66.8.3337-3343.2000 · Cited by 171
Characterisation of sodium caseinate as a function of ionic strength, pH and temperature using static and dynamic light scattering
Hadjsadok, A., Pitkowski, A., Nicolaï, T., et al. (2007) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2007.09.002 · Cited by 169
Préparation de phosphocaséinate natif par microfiltration sur membrane
Pierre, A., Fauquant, J., Graet, Y. L., Piot, M., & Maubois, J. (1992) · Le Lait · doi:10.1051/lait:1992534 · Cited by 168
The effect of thermosonication of milk on selected physicochemical and microstructural properties of yoghurt gels during fermentation
Riener, J., Noci, F., Cronin, D. A., et al. (2008) · Food Chemistry · doi:10.1016/j.foodchem.2008.10.037 · Cited by 164
Formation and structure of acidified milk gels
Horne, D. S. (1999) · International Dairy Journal · doi:10.1016/s0958-6946(99)00072-2 · Cited by 164
Combined effects of temperature and high-pressure treatments on physicochemical characteristics of skim milk
Gaucheron, F., Famelart, M., Mariette, F., et al. (1997) · Food Chemistry · doi:10.1016/s0308-8146(96)00301-9 · Cited by 163
Self-citation
The use of ultrafiltration and dialysis in isolating the aqueous phase of milk and in determining the partition of milk constituents between the aqueous and disperse phases
Davies, D. T., & White, J. C. D. (1960) · Journal of Dairy Research · doi:10.1017/s0022029900010256 · Cited by 157
Mineral and casein equilibria in milk: effects of added salts and calcium-chelating agents
Udabage, P., McKINNON, I. R., & Augustin, M.-A. (2000) · Journal of Dairy Research · doi:10.1017/s0022029900004271 · Cited by 155
Skim Milk Acidification
de Kruif, C. G. (1997) · Journal of Colloid and Interface Science · doi:10.1006/jcis.1996.4548 · Cited by 151
Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)lysine and the susceptibility of individual proteins towards crosslinking
Sharma, R., Lorenzen, P. C., & Qvist, K. B. (2001) · International Dairy Journal · doi:10.1016/s0958-6946(01)00096-6 · Cited by 143
Relationship Between Physical Properties of Casein Micelles and Rheology of Skim Milk Concentrate
Karlsson, A. O., Ipsen, R., Schrader, K., & Ardö, Y. (2005) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(05)73064-2 · Cited by 138
PHYSICOCHEMICAL AND STRUCTURAL CHARACTERISTICS OF SODIUM CASEINATE BIOPOLYMERS INDUCED BY MICROBIAL TRANSGLUTAMINASE
Tang, C., Yang, X., Chen, Z., et al. (2005) · Journal of Food Biochemistry · doi:10.1111/j.1745-4514.2005.00038.x · Cited by 137
Physical, chemical and biochemical properties of casein hydrolyzed by three proteases: Partial characterizations
Luo, Y., Pan, K., & Zhong, Q. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.01.048 · Cited by 136
Déshydratation par atomisation de phosphocaséinate natif obtenu par microfiltration sur membrane
Schuck, P., Piot, M., Méjean, S., et al. (1994) · Le Lait · doi:10.1051/lait:1994531 · Cited by 135
Les équilibres minéraux du lait : influence du pH et de la force ionique
Graët, Y. L., & Brulé, G. (1993) · Le Lait · doi:10.1051/lait:199312 · Cited by 133
Heat-induced interactions of β-lactoglobulin and α-lactalbumin with the casein micelle in pH-adjusted skim milk
Oldfield, D. J., Singh, H., Taylor, M. W., et al. (2000) · International Dairy Journal · doi:10.1016/s0958-6946(00)00087-x · Cited by 132
Rheological Properties of Yoghurt Made with Milk Submitted to Manothermosonication
Vercet, A., Oria, R., Marquina, P. L., et al. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0204654 · Cited by 132
The temperature-dependent dissociation of β-casein from bovine casein micelles and complexes
DOWNEY, W. K., & Murphy, R. F. (1970) · Journal of Dairy Research · doi:10.1017/s002202990001339x · Cited by 130
Stability of Casein Micelles Cross-Linked by Transglutaminase
Smiddy, M. A., Martin, J.-E. G. H., Kelly, A. L., et al. (2006) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(06)72258-5 · Cited by 129
Effect of calcium chelators on physical changes in casein micelles in concentrated micellar casein solutions
de Kort, E., Minor, M., Snoeren, T. J., et al. (2011) · International Dairy Journal · doi:10.1016/j.idairyj.2011.06.007 · Cited by 127
Interactions between tea catechins and casein micelles and their impact on renneting functionality
Haratifar, S., & Corredig, M. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.07.092 · Cited by 125
Protein‐glutaminase from Chryseobacterium proteolyticum, an enzyme that deamidates glutaminyl residues in proteins
Yamaguchi, S., Jeenes, D. J., & Archer, D. B. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02019.x · Cited by 124
Structure and stability of nanogel particles prepared by internal cross-linking of casein micelles
Huppertz, T., & de Kruif, C. G. (2007) · International Dairy Journal · doi:10.1016/j.idairyj.2007.10.009 · Cited by 122
Physicochemical characterization of calcium-supplemented skim milk
Philippe, M., Gaucheron, F., Graët, Y. L., Michel, F., & Garem, A. (2003) · Le Lait · doi:10.1051/lait:2002049 · Cited by 122
Self-citation
Study of Acid and Rennet Coagulation of High Pressurized Milk
Desobry-Banon, S., Richard, F., & Hardy, J. (1994) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(94)77267-2 · Cited by 120
Impaired rennetability of heated milk; study of enzymatic hydrolysis and gelation kinetics.
Vasbinder, A. J., Rollema, H., & de Kruif, C. D. (2003) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(03)73740-0 · Cited by 116
The effects of different cations on the physicochemical characteristics of casein micelles
Philippe, M., Legraet, Y., & Gaucheron, F. (2005) · Food Chemistry · doi:10.1016/j.foodchem.2004.06.001 · Cited by 116
Self-citation
Deamidation of food proteins to improve functionality
Hamada, J. S., & Swanson, B. (1994) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408399409527664 · Cited by 115
Solvent-Mediated Disruption of Bovine Casein Micelles at Alkaline pH
Vaia, B., Smiddy, M. A., Kelly, A. L., et al. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf061417c · Cited by 115
pH-induced solubilization of minerals from casein micelles: influence of casein concentration and ionic strength
Graët, Y. L., & Gaucheron, F. (1999) · Journal of Dairy Research · doi:10.1017/s0022029999003386 · Cited by 114
Self-citation
Preparation, characterisation and selected functional properties of sodium caseinate–maltodextrin conjugates
O’Regan, J., & Mulvihill, D. M. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2009.01.045 · Cited by 111
Characterization of casein hydrolysates derived from enzymatic hydrolysis
Wang, J., Su, Y., Jia, F., & Jin, H. (2013) · Chemistry Central Journal · doi:10.1186/1752-153x-7-62 · Cited by 111
Effects of Enzymatic Deamidation by Protein-Glutaminase on Structure and Functional Properties of α-Zein
Yong, Y. H., Yamaguchi, S., Gu, Y. S., et al. (2004) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf040133u · Cited by 110
The Milk Salts and Their Interaction with Casein
Holt, C. (1997) · Springer eBooks · doi:10.1007/978-1-4757-4409-5_6 · Cited by 106
Functional properties of milk protein concentrates: Emulsifying properties, adsorption and stability of emulsions
Ye, A. (2010) · International Dairy Journal · doi:10.1016/j.idairyj.2010.07.005 · Cited by 105
Effect of Trisodium Citrate on Rheological and Physical Properties and Microstructure of Yogurt
Ozcan-Yilsay, T., Lee, W.-J., Horne, D. S., & Lucey, J. A. (2007) · Journal of Dairy Science · doi:10.3168/jds.2006-538 · Cited by 102
Transglutaminase: effect on rheological properties, microstructure and permeability of set style acid skim milk gel
Færgemand, M., & Qvist, K. B. (1997) · Food Hydrocolloids · doi:10.1016/s0268-005x(97)80058-6 · Cited by 101
Effect of Oxalate and Urea upon Ultracentrifugation Properties of Raw and Heated Skimmilk Casein Micelles
Morr, C. V. (1967) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(67)87710-5 · Cited by 100
Biocompatible Micro-Gel Particles from Cross-Linked Casein Micelles
Huppertz, T., Smiddy, M. A., & de Kruif, C. G. (2007) · Biomacromolecules · doi:10.1021/bm061070m · Cited by 99
Influence of glycosylation on micelle-stabilizing ability and biological properties of C-terminal fragments of cow's κ-casein
Dziuba, J., & Mińkiewicz, P. (1996) · International Dairy Journal · doi:10.1016/0958-6946(95)00074-7 · Cited by 98
Rehydration of casein powders: effects of added mineral salts and salt addition methods on water transfer
Schuck, P., Davenel, A., Mariette, F., et al. (2002) · International Dairy Journal · doi:10.1016/s0958-6946(01)00090-5 · Cited by 97
Influence of transglutaminase treatment on some physico-chemical properties of milk
O'SULLIVAN, M. M., Kelly, A. L., & Fox, P. F. (2002) · Journal of Dairy Research · doi:10.1017/s0022029902005617 · Cited by 96
Dairy-Derived Ingredients: Food And Nutraceutical Uses
Corredig, M. (2014) · Medical Entomology and Zoology · Cited by 95
The Constituents of Gardenia jasminoides Geniposide and Genipin-gentiobioside
Endo, T., & TAGUCHI, H. (1973) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.21.2684 · Cited by 95
Emulsifying Properties of Milk Proteins Cross-linked with Microbial Transglutaminase
Færgemand, M., Otte, J., & Qvist, K. B. (1998) · International Dairy Journal · doi:10.1016/s0958-6946(98)00111-3 · Cited by 95
Chemical Modifications on Proteins Using Glutaraldehyde
Silva, C., Sousa, F., Gübitz, G., et al. (2004) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) · Cited by 93
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
Composition of Ultrafiltrates from Milk Heated at 80 to 230° F. in Relation to Heat Stability
Rose, D., & Tessier, H. (1959) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(59)90680-0 · Cited by 92
Effects of pH and temperature on the milk salt system
Visser, J., Minihan, A. R., Smits, P., et al. (1986) · Netherlands milk and dairy journal · Cited by 92
Effect of NaCl on some physico-chemical properties of concentrated bovine milk
Huppertz, T., & Fox, P. F. (2006) · International Dairy Journal · doi:10.1016/j.idairyj.2005.09.011 · Cited by 91
Enzymatic modification of milk protein concentrate and characterization of resulting functional properties
Banach, J. C., Lin, Z., & Lamsal, B. P. (2013) · LWT · doi:10.1016/j.lwt.2013.06.023 · Cited by 91
Modern Mass Spectrometric Methodologies in Monitoring Milk Quality
Siciliano, R. A., Rega, B., Amoresano, A., et al. (1999) · Analytical Chemistry · doi:10.1021/ac990590n · Cited by 91
Studies of casein micelle structure: the past and the present
Qi, P. X. (2007) · Le Lait · doi:10.1051/lait:2007026 · Cited by 91
Characterisation of bla TEM genes and types of β-lactamase plasmids in Neisseria gonorrhoeae – the prevalent and conserved bla TEM-135 has not recently evolved and existed in the Toronto plasmid from the origin
Muhammad, I., Golparian, D., Dillon, J. R., et al. (2014) · BMC Infectious Diseases · doi:10.1186/1471-2334-14-454 · Cited by 90
Effect of heat treatment on the physical properties of milk gels made with both rennet and acid
Lucey, J. A., Tamehana, M., Singh, H., & Munro, P. A. (2001) · International Dairy Journal · doi:10.1016/s0958-6946(01)00081-4 · Cited by 90
Reconstitution properties of micellar casein powder: Effects of composition and storage
Schokker, E. P., Church, J. S., Mata, J. P., et al. (2011) · International Dairy Journal · doi:10.1016/j.idairyj.2011.05.004 · Cited by 89
Protein interactions in heat-treated milk and effect on rennet coagulation
Kethireddipalli, P., Hill, A. R., & Dalgleish, D. G. (2010) · International Dairy Journal · doi:10.1016/j.idairyj.2010.06.003 · Cited by 89
Mineral and protein equilibria between the colloidal and soluble phases of milk at low temperature
Pierre, A., & Brulé, G. (1981) · Journal of Dairy Research · doi:10.1017/s0022029900021890 · Cited by 89
pH-Induced physicochemical modifications of native phosphocaseinate suspensions: Influence of aqueous phase
Famelart, M. H., Lepesant, F., Gaucheron, F., et al. (1996) · Le Lait · doi:10.1051/lait:1996534 · Cited by 89
Self-citation
Scattering and Turbidity Study of the Dissociation of Casein by Calcium Chelation
Pitkowski, A., Nicolaï, T., & Durand, D. (2007) · Biomacromolecules · doi:10.1021/bm7006899 · Cited by 88
Microstructural changes in casein supramolecules during acidification of skim milk
McMahon, D. J., Du, H., McManus, W. R., et al. (2009) · Journal of Dairy Science · doi:10.3168/jds.2009-2324 · Cited by 87
Functional properties of food proteins polymerized by transglutaminase.
Motoki, M., Nio, N., & Takinami, K. (1984) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.48.1257 · Cited by 86
Ultrasound improves the renneting properties of milk
(2014) · doi:10.1016/j.ultsonch.2014.03.034 · Cited by 84
pH-induced demineralization of casein micelles modifies their physico-chemical and foaming properties
Silva, N. F. N., Piot, M., de Carvalho, A. F., et al. (2013) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2013.01.004 · Cited by 84
Influence of Processing on Functionality of Milk and Dairy Proteins
Augustin, M. A., & Udabage, P. (2007) · Advances in food and nutrition research · doi:10.1016/s1043-4526(07)53001-9 · Cited by 83
Acid-induced gelation behavior of sonicated casein solutions
Madadlou, A., Emam‐Djomeh, Z., Mousavi, M., Mohamadifar, M., & Ehsani, M. (2009) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2009.06.009 · Cited by 82
Influence of mixtures of calcium-chelating salts on the physicochemical properties of casein micelles
Kaliappan, S., & Lucey, J. A. (2011) · Journal of Dairy Science · doi:10.3168/jds.2010-3343 · Cited by 82
Sonodisruption of re-assembled casein micelles at different pH values
Madadlou, A., Mousavi, M., Emam‐Djomeh, Z., et al. (2009) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2008.12.018 · Cited by 81
Development of Casein Microgels from Cross-Linking of Casein Micelles by Genipin
Silva, N. F. N., Saint‐Jalmes, A., de Carvalho, A. F., et al. (2014) · Langmuir · doi:10.1021/la502274b · Cited by 81
A model for predicting salt equilibria in milk and mineral-enriched milks
Mekmene, O., Graët, Y. L., & Gaucheron, F. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2009.02.039 · Cited by 81
Self-citation
Phosphorylation of casein and lysozyme by phosphorus oxychloride
Matheis, G., Penner, M. H., Feeney, R. E., et al. (1983) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00116a049 · Cited by 81
Properties of casein micelles in high pressure-treated bovine milk
Huppertz, T., Fox, P. F., & Kelly, A. L. (2003) · Food Chemistry · doi:10.1016/j.foodchem.2003.10.025 · Cited by 80
Characterization of heat-induced lactosylation products in caseins by immunoenzymatic and mass spectrometric methodologies
Scaloni, A., Perillo, V., Franco, P., et al. (2002) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s0167-4838(02)00290-x · Cited by 80
Collagen-Based Fibrillar Multilayer Films Cross-Linked by a Natural Agent
Chaubaroux, C., Vrana, N. E., Debry, C., et al. (2012) · Biomacromolecules · doi:10.1021/bm300529a · Cited by 79
pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. 2. Effect of pH on renneting of milk
van Hooydonk, A. C. M., Boerrigter, I. J., & Hagedoorn, H. G. (1986) · Netherlands milk and dairy journal · Cited by 79
Effects of different calcium salts on properties of milk related to heat stability
Omoarukhe, E. D., On‐Nom, N., Grandison, A. S., et al. (2010) · International Journal of Dairy Technology · doi:10.1111/j.1471-0307.2010.00613.x · Cited by 77
Characterization and improvement of rheological properties of sodium caseinate glycated with galactose, lactose and dextran
Corzo‐Martínez, M., Moreno, F. J., Villamiel, M., et al. (2009) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2009.08.008 · Cited by 76
Direct evidence for the role of Maillard reaction products in protein cross-linking in milk powder during storage
Le, T. T., Holland, J. W., Bhandari, B., et al. (2013) · International Dairy Journal · doi:10.1016/j.idairyj.2013.02.013 · Cited by 76
Steric stabilization and casein micelle stability
Horne, D. S. (1986) · Journal of Colloid and Interface Science · doi:10.1016/0021-9797(86)90024-x · Cited by 76
Casein micelle dispersions into water, NaCl and CaCl2: physicochemical characteristics of micelles and rennet coagulation
Famelart, M., Graet, Y. L., & Raulot, K. (1999) · International Dairy Journal · doi:10.1016/s0958-6946(99)00077-1 · Cited by 75
Determination of heat-induced effects on the particle size distribution of casein micelles by dynamic light scattering and nanoparticle tracking analysis
Le, T. T., Saveyn, P., Hoa, H. D., et al. (2008) · International Dairy Journal · doi:10.1016/j.idairyj.2008.06.006 · Cited by 74
pH-Induced Physico-Chemical Changes of Casein Micelles in Milk and Their Effect on Renneting
van Hooydonk, A. C. M., Hagedoorn, H. G., & Boerrigter, I. J. (1986) · Springer eBooks · doi:10.1007/978-94-009-3733-8_63 · Cited by 72
Properties of dephosphorylated αs1-casein. Precipitation by calcium ions and micelle formation
Bingham, E. W., Farrell, H. M., & Carroll, R. J. (1972) · Biochemistry · doi:10.1021/bi00763a010 · Cited by 72
Effect of deamidation by protein-glutaminase on physicochemical and functional properties of skim milk
Miwa, N., Yokoyama, K.-I., Wakabayashi, H., & Nio, N. (2010) · International Dairy Journal · doi:10.1016/j.idairyj.2009.12.015 · Cited by 72
Dynamics of casein micelles in skim milk during and after high pressure treatment
Orlien, V., Knudsen, J. C., Colon, M., & Skibsted, L. H. (2005) · Food Chemistry · doi:10.1016/j.foodchem.2005.05.082 · Cited by 71
Heat stability of reconstituted casein micelle dispersions: changes induced by salt addition
Ray, C. L., Maubois, J.-L., Gaucheron, F., et al. (1998) · Le Lait · doi:10.1051/lait:1998437 · Cited by 71
Self-citation
EDTA-induced dissociation of casein micelles and its effect on foaming properties of milk
Ward, B. R., Goddard, S. J., Augustin, M.-A., et al. (1997) · Journal of Dairy Research · doi:10.1017/s0022029997002367 · Cited by 69
Proteolysis of milk proteins lactosylated in model systems.
Dalsgaard, T., Nielsen, J. H., & Larsen, L. B. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200600112 · Cited by 68
Effect of acylation on substructural properties of proteins: a study using fluorescence and circular dichroism
Lakkis, J. M., & Villota, R. (1992) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00016a005 · Cited by 68
Ultrasound effects on the assembly of casein micelles in reconstituted skim milk
Liu, Z., Juliano, P., Williams, R. P. W., et al. (2013) · Journal of Dairy Research · doi:10.1017/s0022029913000721 · Cited by 67
On the novel catalytically-independent antimicrobial function of hen egg-white lysozyme: A conformation-dependent activity
Ibrahim, H. R. (1998) · Food / Nahrung · doi:10.1002/(sici)1521-3803(199808)42:03/04 · Cited by 67
Functional Properties and Bitterness of Sodium Caseinate Hydrolysates Prepared with a Bacillus Proteinase
Slattery, H., & Fitzgerald, R. J. (1998) · Journal of Food Science · doi:10.1111/j.1365-2621.1998.tb15755.x · Cited by 67
Interaction of curcumin with phosphocasein micelles processed or not by dynamic high-pressure
Benzaria, A., Maresca, M., Taïeb, N., & Dumay, E. M. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2012.12.017 · Cited by 66
Functional Properties of Food Proteins Polymerized by Transglutaminase
Motoki, M., Nio, N., & Takinami, K. (1984) · Agricultural and Biological Chemistry · doi:10.1080/00021369.1984.10866304 · Cited by 65
Temperature effect on calcium and phosphorus equilibria in relation to gel formation during acidification of skim milk
Koutina, G., Knudsen, J. C., Andersen, U., & Skibsted, L. H. (2014) · International Dairy Journal · doi:10.1016/j.idairyj.2014.01.003 · Cited by 64
Effect of Ultra‐high Temperature Treatment on the Enzymatic Cross‐linking of Micellar Casein and Sodium Caseinate by Transglutaminase
Bönisch, M. P., Lauber, S., & Kulozik, U. (2004) · Journal of Food Science · doi:10.1111/j.1365-2621.2004.tb09902.x · Cited by 64
Temperature-dependent dynamics of bovine casein micelles in the range 10–40°C
Liu, Z., Weeks, M. G., Dunstan, D. E., et al. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.06.130 · Cited by 64
Effect of adding salt during the diafiltration step of milk protein concentrate powder manufacture on mineral and soluble protein composition
Sikand, V., Tong, P. S., & Walker, J. (2013) · Dairy Science and Technology · doi:10.1007/s13594-013-0110-0 · Cited by 64
Enzymic dephosphorylation of bovine casein to improve acid clotting properties and digestibility for infant formula
Li‐Chan, E. C. Y., & Nakai, S. (1989) · Journal of Dairy Research · doi:10.1017/s0022029900028843 · Cited by 64
Mass spectrometry for the analysis of protein lactosylation in milk products
Siciliano, R. A., Mazzeo, M. F., Arena, S., Renzone, G., & Scaloni, A. (2012) · Food Research International · doi:10.1016/j.foodres.2012.10.044 · Cited by 63
Enhanced delivery of baicalein using cinnamaldehyde cross-linked chitosan nanoparticle inducing apoptosis
Babu, V. N., & Kannan, S. (2012) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2012.08.038 · Cited by 62
Glutamine-specific deamidation of .ALPHA.S1-casein by transglutaminase.
Motoki, M., Seguro, K., Nio, N., et al. (1986) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.50.3025 · Cited by 62
Influence of transglutaminase treatment on properties of micellar casein and products made therefrom
Mounsey, J. S., O’Kennedy, B. T., & Kelly, P. M. (2005) · Le Lait · doi:10.1051/lait:2005028 · Cited by 59
Gelation mechanism of protein solution by transglutaminase.
Nio, N., Motoki, M., & Takinami, K. (1986) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.50.851 · Cited by 59
Physico-chemical changes in casein micelles of buffalo and cow milks as a function of alkalinisation
Ahmad, S., Piot, M., Rousseau, F., et al. (2009) · Dairy Science and Technology · doi:10.1051/dst/2009020 · Cited by 58
Phosphorylation of food proteins with phosphorus oxychloride—Improvement of functional and nutritional properties: A review
MATHEIS, G. (1991) · Food Chemistry · doi:10.1016/0308-8146(91)90081-x · Cited by 57
Increased loading of vitamin D 2 in reassembled casein micelles with temperature-modulated high pressure treatment
Menéndez-Aguirre, O., Kessler, A., Stuetz, W., Grune, T., Weiß, J., & Hinrichs, J. (2014) · Food Research International · doi:10.1016/j.foodres.2014.06.010 · Cited by 57
Heat-induced deamidation, dephosphorylation and breakdown of caseinate
van Boekel, M. A. J. S. (1999) · International Dairy Journal · doi:10.1016/s0958-6946(99)00068-0 · Cited by 56
Effect of casein micelle composition and casein dephosphorylation on coagulation and syneresis
Pearse, M. J., Linklater, P. M., Hall, R. J., et al. (1986) · Journal of Dairy Research · doi:10.1017/s0022029900025000 · Cited by 55
Processing of phosphocasein dispersions by dynamic high pressure: Effects on the dispersion physico-chemical characteristics and the binding of α-tocopherol acetate to casein micelles
Chevalier‐Lucia, D., Blayo, C., Gràcia-Julià, A., et al. (2011) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2011.07.007 · Cited by 53
Effect of Controlled κ-Casein Hydrolysis on Rheological Properties of Acid Milk Gels
Gastaldi, E., Trial, N., Guillaume, C., Bourret, E., Gontard, N., & Cuq, J. L. (2003) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(03)73650-9 · Cited by 52
Rheological and structural properties of differently acidified and renneted milk gels
Liu, X., Zhang, H., Wang, F., Luo, J., Guo, H., & Ren, F. (2014) · Journal of Dairy Science · doi:10.3168/jds.2013-7568 · Cited by 52
Covalent binding of glycosyl residues to bovine casein: effects on solubility and viscosity
Courthaudon, J. L., Colas, B., & Lorient, D. (1989) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00085a008 · Cited by 51
Influence of Milk Peptides in Determining the Functionality of Milk Proteins: A Review
Haque, Z. U. (1993) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(93)77352-x · Cited by 50
Reformation of casein particles from alkaline-disrupted casein micelles
Huppertz, T., Vaia, B., & Smiddy, M. A. (2008) · Journal of Dairy Research · doi:10.1017/s0022029907002956 · Cited by 50
Dephosphorylation of αS- and κ-Caseins and Its Effect on Micelle Stability in the κ-αS-Casein System
Pepper, L., & Thompson, M. P. (1963) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(63)89145-6 · Cited by 49
Influence of enzymatic cross-linking on milk fat globules and emulsifying properties of milk proteins
Hinz, K., Huppertz, T., Kulozik, U., et al. (2006) · International Dairy Journal · doi:10.1016/j.idairyj.2006.05.001 · Cited by 48
Iron-supplemented caseins: preparation, physicochemical characterization and stability
Gaucheron, F., Famelart, M., & Graët, Y. L. (1996) · Journal of Dairy Research · doi:10.1017/s0022029900031733 · Cited by 48
Self-citation
Gelation Mechanism of Protein Solution by Transglutaminase
Nio, N., Motoki, M., & Takinami, K. (1986) · Agricultural and Biological Chemistry · doi:10.1080/00021369.1986.10867499 · Cited by 47
Theoretical Model for Calculating Ionic Equilibria in Milk as a Function of pH: Comparison to Experiment
Mekmene, O., Graët, Y. L., & Gaucheron, F. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf903628r · Cited by 47
Self-citation
Binding of cations to casein molecules: Importance of physico-chemical conditions
Gaucheron, F., Graët, Y. L., Boyaval, E., et al. (1997) · HAL (Le Centre pour la Communication Scientifique Directe) · Cited by 47
Self-citation
Effect of heating and cooling on the milk salts and their interaction with casein
Holt, C. (1995) · Bulletin. International Dairy Federation · Cited by 45
Action of Protein-Glutaminase on α-Lactalbumin in the Native and Molten Globule States
Gu, Y. S., Matsumura, Y., Yamaguchi, S., et al. (2001) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf010287z · Cited by 45
Glycation of caseinate by fructose and fructo‐oligosaccharides during controlled heat treatment in the ‘dry’ state
Oliver, C. M., Melton, L. D., & Stanley, R. A. (2005) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.2405 · Cited by 45
Effects of addition of phenolic compounds on the acid gelation of milk
Harbourne, N., Jacquier, J., & O’Riordan, D. (2010) · International Dairy Journal · doi:10.1016/j.idairyj.2010.10.003 · Cited by 45
High pressure-assisted encapsulation of vitamin D2in reassembled casein micelles
Menéndez-Aguirre, O., Stuetz, W., Grune, T., et al. (2011) · High Pressure Research · doi:10.1080/08957959.2011.565057 · Cited by 45
Relationship Between Blocked Lysine and Carbohydrate Composition of Infant Formulas
Evangelisti, F., Calcagno, C., & Zunin, P. (1994) · Journal of Food Science · doi:10.1111/j.1365-2621.1994.tb06961.x · Cited by 44
Calcium and phosphate partitions during the manufacture of sterilized concentrated milk and their relations to the heat stability
Timmermans, W., & Walstra, P. (1988) · Netherlands milk and dairy journal · Cited by 44
Acylated β-Caseins: Electrostatic Interactions and Aggregation
Hoagland, P. D. (1966) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(66)87945-6 · Cited by 43
The physical characteristics and emulsification properties of partially dephosphorylated bovine β-casein
McCarthy, N. A., Kelly, A. L., O’Mahony, J. A., et al. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2012.11.080 · Cited by 42
Characterization of high-milk-protein powders upon rehydration under various salt concentrations
Hussain, R., Gaïani, C., Aberkane, L., et al. (2010) · Journal of Dairy Science · doi:10.3168/jds.2010-3323 · Cited by 41
High pressure effects on the colloidal calcium phosphate and the structural integrity of micellar casein in milk. II. Kinetics of the casein micelle disintegration and protein interactions in milk
Schrader, K., & Buchheim, W. (1998) · Kieler Milchwirtschaftliche Forschungsberichte · Cited by 41
Changes in the physico-chemical properties of casein micelles during ultrafiltration combined with diafiltration
(2014) · doi:10.1016/j.lwt.2014.04.037 · Cited by 40
Use of cold microfiltration to produce unique ?-casein enriched milk gels
Hekken, D. L. V., & Holsinger, V. H. (2000) · Le Lait · doi:10.1051/lait:2000108 · Cited by 40
Properties of casein micelles cross‐linked by transglutaminase
Moon, J.-H., Hong, Y., Huppertz, T., et al. (2009) · International Journal of Dairy Technology · doi:10.1111/j.1471-0307.2008.00442.x · Cited by 38
Physicochemical characterization of iron-supplemented skim milk
Gaucheron, F., Graët, Y. L., Raulot, K., et al. (1997) · International Dairy Journal · doi:10.1016/s0958-6946(96)00054-4 · Cited by 38
Self-citation
Pressurisation of raw skim milk and of a dispersion of phosphocaseinate at 9 °C or 20 °C: effects on the distribution of minerals and proteins between colloidal and soluble phases
Regnault, S., Dumay, E. M., & Cheftel, J. C. (2006) · Journal of Dairy Research · doi:10.1017/s0022029905001494 · Cited by 38
Emulsifying properties of peptides obtained from the hydrolyzates of .BETA.-casein.
Soo Won, L. E. E., Shimizu, M., Kaminogawa, S., et al. (1987) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.51.161 · Cited by 38
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
Role of Phosphate Groups in the Calcium Sensitivity of αs2-Casein
Aoki, T., Toyooka, K., & Kako, Y. (1985) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(85)81005-5 · Cited by 36
Effect of milk caseins on the concentration of polyphenolic compounds in tea
Kartsova, L. A., & Alekseeva, A. V. (2008) · Journal of Analytical Chemistry · doi:10.1134/s1061934808110154 · Cited by 35
Complexing of Calcium by Hexametaphosphate, Oxalate, Citrate, and Ethylenediamine-Tetraacetate in Milk. II. Dialysis of Milk Containing Complexing Agents
Odagiri, S., & NICKERSON, T. A. (1965) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(65)88153-x · Cited by 34
Dephosphorylation of bovine casein by milk alkaline phosphatase
Lorient, D., & Linden, G. (1976) · Journal of Dairy Research · doi:10.1017/s0022029900015557 · Cited by 34
Effect of Added NaCl on Some Physicochemical Properties of Milk
Grufferty, M. B., & Fox, P. F. (2016) · Cited by 34
Fermented Milk Products
Mayo, B., Ammor, M. S., Delgado, S., & Alegría, Á. (2010) · doi:10.1201/ebk1420094954-13 · Cited by 34
Effect of NaCl addition on the mineral equilibrium of concentrated and acidified casein micelles
Gaucheron, F., Graët, Y. L., & Briard, V. (2000) · HAL (Le Centre pour la Communication Scientifique Directe) · Cited by 32
Self-citation
Casein micelles as a vehicle for iron fortification of foods
Raouche, S., Dobenesque, M., Bot, A., et al. (2009) · European Food Research and Technology · doi:10.1007/s00217-009-1130-0 · Cited by 32
Skim milk powders with enhanced foaming and steam-frothing properties
Augustin, M. A., & Clarke, P. T. (2008) · Dairy Science and Technology · doi:10.1051/dst:2007012 · Cited by 32
Improvement of the pH-solubility profile of sodium caseinate by using Ca2+-independent microbial transglutaminase with gelatin
Nonaka, M., Matsuura, Y., Nakano, K., et al. (1997) · Food Hydrocolloids · doi:10.1016/s0268-005x(97)80065-3 · Cited by 31
Effect of dephosphorylation on bovine casein
Molina, A. C. T., Alli, I., Konishi, Y., & Kermasha, S. (2006) · Food Chemistry · doi:10.1016/j.foodchem.2006.03.033 · Cited by 31
study of the dissociation of beta casein from the bovine casein micelle at low temperature
Creamer, L. K., Berry, G. P., & Mills, O. E. (1977) · Journal of Dairy Science and Technology · Cited by 30
A model for the assembly of bovine casein micelles from F2 and F3 subunits
Ono, T., & Obata, T. (1989) · Journal of Dairy Research · doi:10.1017/s0022029900028934 · Cited by 29
Effect of enzymatic deamidation by protein-glutaminase on the textural and microstructural properties of set yoghurt
Miwa, N., Nio, N., & Sonomoto, K. (2013) · International Dairy Journal · doi:10.1016/j.idairyj.2013.12.002 · Cited by 28
Effects of some calcium-chelating agents on the physical properties of acid-set milk gels
Johnston, D. E., & Murphy, R. J. (1992) · Journal of Dairy Research · doi:10.1017/s0022029900030442 · Cited by 28
AFM study of casein micelles cross-linked by genipin: effects of acid pH and citrate
Silva, N. F. N., Bahri, A., Guyomarc’H, F., Beaucher, E., & Gaucheron, F. (2014) · Dairy Science and Technology · doi:10.1007/s13594-014-0199-9 · Cited by 28
Self-citation
Acidification of pressure-treated milk
Famelart, M. H., Gaucheron, F., Mariette, F., et al. (1997) · International Dairy Journal · doi:10.1016/s0958-6946(97)00021-6 · Cited by 27
Self-citation
Disruption and reassociation of casein micelles during high pressure treatment: influence of whey proteins
Huppertz, T., & de Kruif, C. G. (2007) · Journal of Dairy Research · doi:10.1017/s0022029906002263 · Cited by 27

Research works printed but not linked: 17

Buccheim W, Prokopeck D (1992) Die Hochdruckbehandlung: ein alternatives Verfahren zur Haltbarmachung und Bearteitung von Milch und anderen Lebensmitteln. Dtsch Milchwirtsch 43:1374–1376
Chobert JM (2012) Milk protein tailoring to improve functional and biological properties. J Bio Sci Biotech 1:171–197
Creamer LK, Roeper J, Lohrey EH (1971) Preparation and evaluation of some acid soluble casein derivatives. N Z J Dairy Sci Technol 6:107
De Kruif CG (2003) Non-food applications of caseins. In WY Aalbersberg, RJ Hamer, P Jasperse, HHJ de Jongh, CG de Kruif, P Walstra, FA de Wolf (eds) Progress in biotechnology: industrial proteins in perspective, Vol. 23 (pp. 259–263, 269). Amsterdam: Elsevier Science Ltd
Fox PF, Mulvihill DM (1983) Functional properties of caseins, caseinates and casein co-precipitates. In: Physico-chemical aspects of dehydrated protein-rich milk products, IDF Symposium, Helsingor, Denmark, Statens Forsogsmejeri, Hillerod, Denmark (pp. 188–259)
Gaucheron F (2001) Heat-induced deamidation of casein molecules: influence of physicochemical conditions. Milchwissenchaft 56:183–187
Gaucheron F (2004b) Minéraux et produits laitiers. Tec & Doc, Paris
Girerd E, Martin JE, Mesnier D, Lorient D (1984) Influence des modifications chimiques de la caséine sur ses propriétés fonctionnelles. Sci Alim 4:251–257
Ichilczyk-Leone J, Amram Y, Scheind N, Lenoir J (1981) Le refroidissement du lait et son comportement en fromagerie. I. Incidences du refroidissement du lait sur ses caractères physico-chimiques et son comportement vis-à-vis de la présure. Rev Lait Fr 401:7–18
Johnston DE, Austin BA, Murphy RJ (1992) Effects of high pressure on milk. Milchwissenschaft 47:760–763
Knoop AM, Peters KH (1975) Phosphatase activity in acidified milk. Milchwissenschaft 30:674–680
Lieske B (1999) Effects of succinylation on selected physico-chemical properties on native casein micelles in milk. Milchwissenchaft 54:623–627
Lorenzen PC, Schlimme E, Roos N (1998) Crosslinking of sodium caseinate by a microbial transglutaminase. Nahrung 42:151–154 · DOI
Philippe M, Gaucheron F, Le Graët Y (2004) Physicochemical characteristics of calcium supplemented skim milk: comparison of three soluble calcium salts. Milchwissenchaft 59:498–504
Rollema HS (2003) Caseinates. In W. Y. Aalbersberg, R. J. Hamer, P. Jasperse, H. H. J. de Jongh, C. G. de Kruif, P. Walstra, and F. A. de Wolf (Eds.), Progress in biotechnology: industrial proteins in perspective, vol. 23 (pp. 255–259, 269). Amsterdam, Elsevier Science Ltd
Swaisgood HE (1992) Chemistry of the caseins. In: Fox PF (ed) Advanced dairy chemistry: vol 1, 2nd edn. Elsevier Applied Science, Proteins New York, pp 63–110
Van Dijk HJM (1992) The properties of casein micelles. VI: behaviour above pH 9, and implications for the micelle model. Nederlands melk en Zuiveltijdschrift 46:101–113

Sorted by citations

Plant Proteins for Future Foods: A Roadmap
Sim, S. Y. J., SRV, A., Chiang, J. H., & Henry, C. J. (2021) · Foods · doi:10.3390/foods10081967 · Cited by 352
Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis
Hansen, E. B., & Marcatili, P. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.613986 · Cited by 16

See all 347

Authors: Broyard, C., & Gaucheron, F.
Affiliations: Institut Agro Rennes-Angers (FR)
Corresponding author: Gaucheron, Frédéric
Venue: Dairy Science & Technology
Publisher: Springer Science and Business Media LLC
Published: 2015-03-27
Volume: 95
Issue: 6
Pages: 831-862
ISSN: 1958-5586 (ISSN-L)
1958-5594
DOI: 10.1007/s13594-015-0220-y
OpenAlex: W1988420360
Cited by: 347
References: 244
Citations by year: 2026: 28 · 2025: 36 · 2024: 45 · 2023: 36 · 2022: 49 · 2021: 42 · 2020: 43 · 2019: 26 · 2018: 19 · 2017: 16 · 2016: 6
FWCI: 18.25
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
Locations: Dairy Science and Technology (publishedVersion)
HAL (submittedVersion, other-oa)
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
Life Sciences › Agricultural and Biological Sciences › Food Science › Microencapsulation and Drying Processes
Keywords: casein, casein micelles, enzyme modification, chemical modification, physical modification, calcium phosphate, thermal stability, gelation, emulsifying properties, foaming properties, viscosity, protein aggregation, hydrophobicity, milk protein

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

Modifications of structures and functions of caseins: a scientific and technological challenge.

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks