The influence of isothermal heat treatments on the adsorption of anionic carrageenan molecules to the surfaces of anionic β-lactoglobulin-coated droplets has been investigated. The ζ-potential, mean particle diameter, microstructure, and creaming stability of emulsions containing β-lactoglobulin-coated droplets and/or carrageenan molecules that had previously been heat treated at temperatures ranging from 30 to 90 °C for 20 min were measured (pH 6.0, 150 mM NaCl). Three different heat treatments were used to establish the physicochemical origin of the influence of thermal history on the adsorption of carrageenan molecules to the protein coated droplets:  (i) droplets and carrageenan were mixed at room temperature, then heated together; (ii) droplets were heated, cooled to room temperature, then mixed with carrageenan; (iii) carrageenan was heated, cooled to room temperature, then mixed with droplets. For treatments i and ii appreciably more carrageenan adsorbed to the protein-coated droplet surfaces at temperatures ≤ 60 °C than at higher temperatures. For treatment iii, carrageenan adsorbed to the droplet surfaces across the whole temperature range. These results suggest that an irreversible thermal denaturation of the adsorbed β-lactoglobulin molecules inhibited the adsorption of carrageenan molecules to the droplet surfaces. We postulate that there is a patch of positive charge on the surface of the native globular protein molecules which becomes more diffuse upon thermal denaturation. We found that the carrageenan molecules were unable to protect the β-lactoglobulin-coated droplets at high temperatures (T > 60 °C) because they desorbed from the droplet surfaces. Nevertheless, adsorption of ι-carrageenan was capable of protecting the droplets against flocculation caused by surface denaturation of the adsorbed proteins at lower temperatures (T ≤ 50 °C).