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 accessOverview
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
Cites
Statistics
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“A median size of 150 nM has been reported for cow milk whereas camel milk has considerable larger casein micelles (Horne, 2008; Broyard and Gaucheron, 2015).”
From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Broyard and Gaucheron, 2015
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Caseins are organized into micelles of quite variable size.”
From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Broyard and Gaucheron, 2015
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Items 201–244 of 244
Morr, C. V. (1967) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(67)87561-1 · Cited by 27
Merel-Rausch, E., Kulozik, U., & Hinrichs, J. (2007) · Journal of Dairy Research · doi:10.1017/s002202990700252x · Cited by 26
Pouliot, Y. (2004) · International Dairy Journal · doi:10.1016/j.idairyj.2004.04.001 · Cited by 25
Chobert, J., Briand, L., Tran, V., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8627 · Cited by 24
Physicochemical and Dynamic Properties of Caseins Modified by Chemical Phosphorylation
Medina, A., Colas, B., Meste, M. L., et al. (1992) · Journal of Food Science · doi:10.1111/j.1365-2621.1992.tb08055.x · Cited by 24
Colas, B., Gobin, C., & Lorient, D. (1988) · Journal of Dairy Research · doi:10.1017/s0022029900033318 · Cited by 24
Modification of casein by phosphatases and protein kinases
Bingham, E. W. (1976) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf60208a015 · Cited by 24
Modification to the renneting functionality of casein micelles caused by nonionic surfactants
Titapiccolo, G. I., Corredig, M., & Alexander, M. (2010) · Journal of Dairy Science · doi:10.3168/jds.2009-2629 · Cited by 23
Effect of lactosylation on plasmin-induced hydrolysis of β-casein
Bhatt, H., Cucheval, A., Coker, C., et al. (2014) · International Dairy Journal · doi:10.1016/j.idairyj.2014.01.017 · Cited by 22
Heterologous gene expression and secretion in Bifidobacterium longum
Park, M., Seo, J., Kim, J., et al. (2005) · Le Lait · doi:10.1051/lait:2004027 · Cited by 22
Schrader, K., Morr, C. V., & Buchheim, W. (1996) · Progress in biotechnology · doi:10.1016/s0921-0423(06)80058-4 · Cited by 21
Effect of Chemical Glycosylation on the Surface Properties of the Soluble Fraction of Casein
Closs, B., COURTHAUDON, J., & Lorient, D. (1990) · Journal of Food Science · doi:10.1111/j.1365-2621.1990.tb06781.x · Cited by 21
An original pH-reversible treatment of milk to improve rennet gelation
Guillaume, C., Jiménez, L., Cuq, J. L., et al. (2003) · International Dairy Journal · doi:10.1016/s0958-6946(03)00149-3 · Cited by 21
Effect of succinylation on the functional properties of yak caseins: a comparison with cow caseins
Yang, M. C., Shi, Y., Wang, P., et al. (2014) · Dairy Science and Technology · doi:10.1007/s13594-014-0168-3 · Cited by 21
Emulsifying Properties of Peptides Obtained from the Hydrolyzates ofβ-Casein
Lee, S. W., Shimizu, M., Kaminogawa, S., et al. (1987) · Agricultural and Biological Chemistry · doi:10.1080/00021369.1987.10867991 · Cited by 21
Study of the dissociation of β-casein from native phosphocaseinate
Pouliot, M., Pouliot, Y., Britten, M., et al. (1994) · Le Lait · doi:10.1051/lait:1994527 · Cited by 20
Micellar Changes in Skimmilk Treated with Alkali or Acid
Odagiri, S., & NICKERSON, T. A. (1965) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(65)88419-3 · Cited by 20
Physicochemical Properties of Acylated Casein Micelles in Milk
Vidal, V., Marchesseau, S., & Cuq, J. L. (2002) · Journal of Food Science · doi:10.1111/j.1365-2621.2002.tb11356.x · Cited by 19
Effect of K‐Casein Deglycosylation on the Acid Coagulability of Milk
Cases, E., Vidal, V., & Cuq, J. L. (2003) · Journal of Food Science · doi:10.1111/j.1365-2621.2003.tb07037.x · Cited by 19
Influence of pH on the heat-induced proteolysis of casein molecules
Gaucheron, F., Mollé, D., & PANNETIER, R. (2001) · Journal of Dairy Research · doi:10.1017/s0022029900004623 · Cited by 19
Self-citationIron fortification of skim milk: Minerals and 57Fe Mössbauer study
Raouche, S., Naille, S., Dobenesque, M., et al. (2008) · International Dairy Journal · doi:10.1016/j.idairyj.2008.07.003 · Cited by 18
Calcium-Binding Property of Dephosphorylated Caseins
YAMAUCHI, K., Takemoto, S., & TSUGÔ, T. (1967) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.31.54 · Cited by 18
Hiller, B., & Lorenzen, P. C. (2008) · LWT · doi:10.1016/j.lwt.2008.06.003 · Cited by 17
Lorenzen, P. C., & Reimerdes, E. H. (1992) · Food / Nahrung · doi:10.1002/food.19920360611 · Cited by 17
Bravo, F. I., Felipe, X., López‐Fandiño, R., et al. (2013) · European Food Research and Technology · doi:10.1007/s00217-012-1902-9 · Cited by 16
Darewicz, M., Dziuba, J., Miodùszewska, H., et al. (1999) · Acta Alimentaria · doi:10.1556/aalim.28.1999.4.5 · Cited by 15
Characterization of casein lactosylation by capillary electrophoresis and mass spectrometry
Steffan, W., Balzer, H. H., Lippert, F., et al. (2005) · European Food Research and Technology · doi:10.1007/s00217-005-0177-9 · Cited by 14
Reimerdes, E. H., & Roggenbuck, G. (1980) · Milk science international/Milchwissenschaft · Cited by 13
Influence of mineral environment on the buffering capacity of casein micelles
Salaun, F. M., Mietton, B., & Gaucheron, F. (2007) · HAL (Le Centre pour la Communication Scientifique Directe) · Cited by 13
Self-citationEffect of dephosphorylation of casein on its coagulation and proteolysis by chymosin.
YAMAUCHI, K., & YONEDA, Y. (1978) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.42.1031 · Cited by 12
The contribution of N-acetylneuraminic acid in the stabilization of micellar casein
Mińkiewicz, P., Dziuba, J., & Muzinska, B. (1993) · Polish Journal of Food and Nutrition Sciences · Cited by 12
Huppertz, T. (2009) · Elsevier eBooks · doi:10.1533/9781845697198.3.394 · Cited by 11
Acylation and Solubility of Casein Precipitated by Carbon Dioxide
dos Santos, C. V. S., & Tomasula, P. M. (2000) · Journal of Food Science · doi:10.1111/j.1365-2621.2000.tb15984.x · Cited by 11
Vidal, V., Marchesseau, S., Lagaude, A., et al. (1998) · Colloids and Surfaces B Biointerfaces · doi:10.1016/s0927-7765(98)00060-5 · Cited by 11
FOAMING PROPERTIES OF MILK PROTEIN CONCENTRATE PREPARED BY ULTRAFILTRATION
Kelly, P. M., & Burgess, K. J. (2016) · Cited by 11
Texture improvement of fermented dairy products by enzymatic crosslinking with transglutaminase
Schey, A. (2003) · International Dairy Federation special issue · Cited by 10
Casiraghi, E., & Lucisano, M. (1991) · Milk science international/Milchwissenschaft · Cited by 10
Enzymatic crosslinking of dairy proteins
Lorenzen, P. C. (2002) · Bulletin. International Dairy Federation · Cited by 9
van Dijk, H. J. M. (1991) · Netherlands milk and dairy journal · Cited by 9
Dependence of the Interfacial Behavior of β-Casein on Phosphoserine Residues
Cassiano, M. M., & Arêas, J. A. G. (2003) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(03)73995-2 · Cited by 8
Rheological Properties and Microstructure of Dephosphorylated Whole Casein Rennet Gels
Hekken, D. L. V., & Strange, E. D. (1994) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(94)77025-9 · Cited by 8
Effects of succinylation on the renneting properties of raw milk.
Lieske, B., Konrad, G., & Faber, W. (2000) · Milk science international/Milchwissenschaft · Cited by 4
N-Glycosidase F improves gel firmness in fermented milk products
Jacobsen, J., Wind, S. L., Rasholt, E. L., et al. (2014) · International Dairy Journal · doi:10.1016/j.idairyj.2013.12.005 · Cited by 3
Hussain, R., Gaïani, C., & Scher, J. (2011) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.1070858 · Cited by 3
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
Cited by
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
Metadata
- Authors
- Broyard, C., & Gaucheron, F.
- Affiliations
- Institut Agro Rennes-Angers (FR)
- Corresponding author
- Gaucheron, Frédéric
- Venue
- Dairy Science & Technology
- Published
- 2015-03-27
- Volume
- 95
- Issue
- 6
- Pages
- 831-862
- ISSN
- 1958-5586 (ISSN-L)
- 1958-5594
- 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
