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

Broyard, Camille; Gaucheron, Frédéric

doi:10.1007/s13594-015-0220-y

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

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

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

DOI 10.1007/s13594-015-0220-y

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A median size of 150 nM has been reported for cow milk whereas camel milk has considerably larger casein micelles.
“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
The Introduction reports an average casein-micelle diameter close to 150 nm, and Table 2 lists a diameter of 150 nm. It does not call that value a median or report a cow–camel comparison; the larger size attributed to camel-milk micelles is therefore unsupported by this source. The paper provides no page numbers for these passages. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Caseins are organized into micelles of quite variable size.
“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

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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
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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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 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

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