Résumé
Casein micelles (CM) are colloidal phospho-protein-mineral complexes naturally present in milk. Cooling inducesβ-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 nanomechanicalsignature 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.