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Solubility, Hydrophobicity and Net Charge of Succinylated Canola Protein Isolate
Author(s) -
PAULSON ALLAN T.,
TUNG MARVIN A.
Publication year - 1987
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.1365-2621.1987.tb05879.x
Subject(s) - succinylation , chemistry , zeta potential , solubility , surface charge , microelectrophoresis , ionic strength , canola , chromatography , aqueous solution , organic chemistry , chemical engineering , biochemistry , amino acid , electrophoresis , food science , lysine , engineering , nanoparticle
Effects of succinylation (54% and 84% modification of free amino groups), pH (3.5–11.0) and NaCl concentration (0.0–0.7M) on solubility, hydrophobicity and zeta potential (net charge) of canola protein isolate were examined. Succinylation markedly enhanced protein solubility at alkaline and slightly acidic pH while effect of NaCl depended on pH. Surface hydrophobicity (S 0 ) decreased as level of succinylation increased. Effect of NaCl varied with pH but in general, S 0 decreased in a curvilinear manner as pH increased. Zeta potential became more electronegative as both succinylation and pH increased, but decreased with addition of NaCl. Hydrophobicity and zeta potential were closely related in a nonlinear inverse manner demonstrating that ionic environment had opposing influences on number of hydrophobic and charged groups on the surface of protein molecules in solution.