Abstract
Significant positive correlations were observed between bound dodecylsulfate or linoleate and dispersibility of surfactant treated soy, sunflower and rapeseed proteins, suggesting that the bound surfactants played an important role in solubilization of these proteins. Dispersibility was also highly correlated with effective hydrophobicity of the proteins as measured fluorometrically. The effective hydrophobicity thus determined for soy, sunflower and rapeseed proteins treated with surfactants and B. subtilis proteinase for solubilization revealed good correlations with surface tension, interfacial tension and emulsifying activity of the proteins, indicating the importance of protein hydrophobicity when used as emulsifiers.
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