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• W2052802988 endingPage "1561" @default.
• W2052802988 startingPage "1557" @default.
• W2052802988 abstract "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 (S0) decreased as level of succinylation increased. Effect of NaCl varied with pH but in general, S0 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." @default.
• W2052802988 created "2016-06-24" @default.
• W2052802988 creator A5046935153 @default.
• W2052802988 creator A5085346251 @default.
• W2052802988 date "1987-11-01" @default.
• W2052802988 modified "2023-10-17" @default.
• W2052802988 title "Solubility, Hydrophobicity and Net Charge of Succinylated Canola Protein Isolate" @default.
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• W2052802988 doi "https://doi.org/10.1111/j.1365-2621.1987.tb05879.x" @default.
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