thermal processing, e.g., cooking, pasteurization or sterilization [11] and [12]. Emulsions stabilized by globular proteins are particularly sensitive to thermal treatments, because these proteins unfold when the temperature exceeds a critical value exposing reactive groups originally located in their interiors, e.g., non-polar or sulfhydryl groups [10•]. These reactive groups increase the attractive interactions between proteins that are adsorbed either on the same or on different droplets, thereby altering the susceptible of emulsions to droplet flocculation and coalescence.
At room temperature, β-lactoglobulin stabilized emulsions (pH 7) are stable to flocculation in the absence of added salt because of the relatively strong electrostatic repulsion between the droplets [9] and [10]•. On the other hand, they become unstable to flocculation when a sufficiently high level of salt (150 mM) is added to the continuous phase because this screens the electrostatic repulsion between the droplets (Fig. 1). At relatively low temperatures (