ABSTRACTThe relationships between protein solubility, surface hydrophobicity (Ho), free sulfhydryl (SHF) and disulfide bond (SSB) content and time of emulsification that determine the emulsion activity index (EAI) and emulsion stability (ES) of five protein additives were investigated at two different ionic strengths (Z = 0.054 and Z = 0.46, pH 6.5). The variables that described EAI at Z = 0.054 were associated with protein disperability and Ho, while protein rigidity factors explained most of the EAI variability at Z = 0.46. The ES models showed similar variable relationships as the EAI models at the same Z. The differences between models at different Z indicated that the relationships between the variables were affected by the ionic strength.
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