Interplay of temperature and calcium content in beta-casein solutions: From controlled self-aggregation of micelles in bulk to the design of stable foams

We describe in this study the aggregation behaviour of β-casein micelles from milk bulk aqueous solution as function both temperature and calcium content, its influence on foaming properties, order to test if different states makes possible design proteins-based thermoresponsive foams. First, we characterized morphology self-assembled molecules by coupling turbidity measurements, Dynamic Light Scattering Small Angle Neutron Scattering. They self-organize into individual at low (20°C) whatever transit a reversible way aggregates large presence calcium, with threshold transition that depend content. The is driven through association serine phosphate groups localized hydrophilic part β-casein. In regime, demonstrated addition tunes number unimers per micelle same than an increase change hydrophobic interactions. chains corona are however good solvent interact excluded volume interactions, even when themselves. internal molecular structure thus not modified bridges, which explains complete reversibility process over cycling. Second, studied foam stability versus time content measuring kinetic evolution liquid fraction. Foams produced solutions containing only were stable terms timescale 1 h 20°C but drained quickly. However, foams become unstable was increased above 20°C. inside channels enabled larger acting cork, slows down drainage. such sufficient long term allow