Emulsification Properties of Succinylated Canola Protein Isolate

Emulsification properties of unmodified and succinylated canola (rapeseed) protein isolate (54 and 84% modification of free amino groups) were examined over a wide range of pH values (pH 3.5–11.0) and sodium chloride concentrations (0.0–0.70M). Both emulsification activity and emulsion stability were increased by succinylation, but extensive succinylation was not required to significantly improve these properties. Multiple regression analyses indicated that emulsification activity was related to protein solubility, hydrophobicity, zeta potential and flow behavior of aqueous dispersions of the proteins. Emulsion stability was affected by protein solubility, zeta potential, apparent viscosity of protein dispersions and difference in density between the aqueous and oil phase.