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
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In the citing paper
“κ-Casein, however, can link only to a hydrophobic residue on another CN molecule. Because it has no phosphoseryl cluster to permit further extension, the polymer chain ends there. No further growth occurs beyond this point. This occurs for each growing chain and hence the proportion of κ-CN limits the micelle size.”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Horne, 1998
In the citing paper
“In consequence, the κ-CN acquires an external surface position where it acts as a steric stabilizer.”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Horne, 1998
In the citing paper
“Decreasing hydrophobic interaction by lowering temperature or increasing electrostatic repulsion by dissolving out Ca phosphate but maintaining pH, disrupts one bonding pathway, weakens also those adjacent bonds and causes (partial) disintegration of the micelle.”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Horne, 1998
In the citing paper
“The solubility of Ca and the CCP equilibrium are also dependent on temperature (Horne, 1998”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Horne, 1998
Citations
Cites
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“, was not signi fi cant, because the binding sites were already exposed due to heat denaturation and unfolding that occurred during the production of whey protein pH disulfide S2 sulfur”
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“The attachment of Ca to caseins through serine phosphate would continue until available serine phosphate is depleted [12].”
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“It seems that various minerals associated with colloidal calcium phosphate (CCP) (Horne, 1998) decreased gradually as CCP was solubilized, although some remained in the colloidal form even at 1 mo of ripening.”
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“The Horne model suggests that acidification of milk leads to solubilization of colloidal calcium phosphate (CCP), which loosens the bridging between caseins, which also disturbs the delicate balance between attraction and repulsion that governs micellar integrity (Horne, 1998).”
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Metadata
- 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)
- 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
- Locations
- International Dairy Journal (publishedVersion)
- Funders
- European Commission
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Milk Quality and Mastitis in Dairy Cows
- Life Sciences › Agricultural and Biological Sciences › Food Science › Animal Diversity and Health Studies
- Keywords
- casein micelles, hydrophobic interactions, electrostatic repulsion, calcium-induced aggregation, acid coagulation, ionic strength effects, temperature effects, pH effect, viscoelasticity, dairy products
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