Article Dans Une Revue Food Hydrocolloids Année : 2026

Comparison of different strategies based on β-casein dynamics to encapsulate curcumin in casein micelles

Résumé

Casein micelles (CM) are colloidal phospho-protein-mineral complexes naturally present in milk. Cooling induces β-casein dissociation from CM. The aim of the present research is to improve curcumin encapsulation in β-casein depleted CM. This study proposes an extraction and separation process including cooling, low acidification (pH 5.8) and membrane filtration at a pilot scale allowing a removal of 45 ±5 % of β-casein fraction from CM. Special care was taken to preserve the CM integrity. Investigation of the depleted CM topography by atomic force microscopy (AFM) reveals a swelling of the micellar structure with a mean width of 193 ±10 nm and a mean height of 80 ±5 nm. Concurrently, exploration of the elastic properties displays a stiffer nanomechanical signature compared to native CM, with a mean elasticity modulus of 195 ±17 kPa. The β-caseins extracted from CM were bound to curcumin prior to their encapsulation in depleted CM. This new encapsulation strategy was compared to two other methods, and the results show that it significantly increases the binding efficiency of curcumin to CM.

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Dates et versions

hal-05370839 , version 1 (18-11-2025)

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Asma Bahri, Marta Martin Fernandez, Csilla Gergely, Sylvie Marchesseau, Dominique Chevalier-Lucia. Comparison of different strategies based on β-casein dynamics to encapsulate curcumin in casein micelles. Food Hydrocolloids, 2026, 173, pp.112258. ⟨10.1016/j.foodhyd.2025.112258⟩. ⟨hal-05370839⟩
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