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Article Dans Une Revue Langmuir Année : 2012

AFM imaging of milk casein micelles: Evidence for structural rearrangement upon acidification

Résumé

Milk casein micelles are natural association colloids that we all encounter in everyday life, yet we still lack an accurate description of their internal structure and the interactions that stabilize it. In this letter, we provide for the first time detailed images of intact casein micelles as obtained through atomic force microscopy under liquid conditions close to physiological. The micelles appear as heterogeneous raspberry-like particles, which is consistent with a hierarchical/spongelike structure made of connected 10−40 nm dense casein regions. Upon in situ acidification to pH 5, the micelles decrease in size and lose their surface heterogeneities, indicating that this structure is highly sensitive to variations in mineral content and caseins net charge.
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Dates et versions

hal-01209301 , version 1 (02-10-2015)

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Mustapha Ouanezar, Fanny Guyomarc'H, Antoine Bouchoux. AFM imaging of milk casein micelles: Evidence for structural rearrangement upon acidification. Langmuir, 2012, 28 (11), pp.4915-4919. ⟨10.1021/la3001448⟩. ⟨hal-01209301⟩
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