Abstract
ABSTRACTEffects 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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
