Casein and casein micelle structures, functions and diversity in 20 species.
Abstract
Primary structures of caseins from 20 species, including two monotremes and two marsupials, have been compared. Sequences of the mature proteins are very divergent, whereas variation in amino acid composition is mostly restricted to a range of disorder-promoting residues. The number and size of clusters of phosphorylation sites in the caseins is variable, blurring the boundaries between them. Casein polar tract sequences were found in all caseins, though of variable lengths, and are chiefly responsible for weak and dynamic interactions among the tangled web of peptide chains in the matrix of casein micelles. The interactions take the predominant form of backbone-to-backbone contacts rather than the sequence-specific side chain interactions of the hydrophobic effect. It is suggested that the dynamic casein micelle matrix be represented by an ensemble of interchanging structures with different types and degrees of inhomogeneity, influenced by solvent quality and other environmental factors.
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The surface of the casein micelle is covered by kappa casein having a hydrophilic glycosylated c-terminal half.
“The surface of the micelle is covered by kappa casein having a hydrophilic glycosylated c-terminal half (Holt, 2016).”
From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Holt, 2016
Section 2.3 (p. 6) describes the C-terminal half of κ-casein as a largely hydrophilic polar tract. Section 3.2 (p. 10) identifies actual or potential glycosylation sites in its macropeptide sequence. The cited passages do not establish that κ-casein covers the micelle surface, and they do not say that the C-terminal half is invariably glycosylated. (LLM, conf=0.85)
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References 104 · Cited by 95
Research works printed but not linked: 1
- Holt, C., Carver, J. A., Ecroyd, H., & Thorn, D. C. (2013). Caseins and the casein micelle: their biological functions, structures and behaviour in foods. Journal of Dairy Science, 96 , 6127-6146.
- Authors
- Holt, C.
- Affiliations
- University of Glasgow (GB)
- Corresponding author
- Holt, Carl
- ORCID
- Holt, Carl
- Venue
- International Dairy Journal
- Publisher
- Elsevier BV
- Published
- 2016-09
- Volume
- 60
- Pages
- 2-13
- ISSN
- 0958-6946 (ISSN-L)
- OpenAlex
- W2272891930
- Cited by
- 95
- References
- 104
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 11 · 2023: 9 · 2022: 10 · 2021: 9 · 2020: 11 · 2019: 10 · 2018: 10 · 2017: 8 · 2016: 2
- FWCI
- 12.60
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- International Dairy Journal (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Animal Diversity and Health Studies
- Keywords
- casein, casein micelles, sequence divergence, amino acid composition, phosphorylation sites, protein disorder, hydrophobic effect, monotremes, marsupials, protein ensembles, solvent quality
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