Emulsifying characteristics of commercial canola protein-hydrocolloid systems
interfacial structure, emulsifying conditions, complex formation, surface-active, molecular interactions
Emulsifying properties of commercial canola protein isolate (CPI)-hydrocolloid-stabilized emulsions were evaluated under varied conditions (CPI, salt and hydrocolloid concentrations; pH, denaturants). Emulsifying activity index (EAI) and emulsion stability (ES) were determined by turbidimetric testing. The results showed that under complexing conditions (at pH 6), the addition of 1% (w/v) κ-carrageenan (κ-CAR) increased the EAI of CPI-stabilized emulsions from 162 to 201 m2/g and ES from 68% to 95%. Under conditions promoting incompatibility (at pH 10), the use of 1% (w/v) guar gum increased the EAI of CPI-stabilized emulsions from 68 to 177 m2/g and ES from 66% to 100%. The lower EAI and ES values observed in CPI-hydrocolloid-stabilized emulsions treated with sodium salts and denaturants support the involvement of hydrophobic interactions, hydrogen bonds and disulfide linkages in the emulsification of these systems. Interfacial properties of CPI-hydrocolloid mixtures were improved by electrostatic complexing and incompatibility, making these systems suitable for stabilizing food emulsions.
Uruakpa, Florence O., and S. D. Arntfield. "Emulsifying characteristics of commercial canola protein–hydrocolloid systems." Food research international 38, no. 6 (2005): 659-672.
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