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Emulsification Properties of Succinylated Canola Protein Isolate
Author(s) -
PAULSON ALLAN T.,
TUNG MARVIN A.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb08961.x
Subject(s) - succinylation , rapeseed , emulsion , chemistry , canola , solubility , zeta potential , chromatography , aqueous solution , aqueous two phase system , isoelectric point , viscosity , chemical engineering , lysine , food science , organic chemistry , biochemistry , amino acid , materials science , nanoparticle , engineering , composite material , enzyme
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.