| Abstract
| - Emulsions were made with sunflower protein isolate (SI), helianthinin, and sunflower albumins (SFAs).Emulsion formation and stabilization were studied as a function of pH and ionic strength and afterheat treatment of the proteins. The emulsions were characterized with respect to average dropletsize, surface excess, and the occurrence of coalescence and/or droplet aggregation. Sunflowerproteins were shown to form stable emulsions, with the exception of SFAs at neutral and alkaline pHvalues. Droplet aggregation occurred in emulsions made with SI, helianthinin, and SFAs. Dropletaggregation and subsequent coalescence of emulsions made with SFAs could be prevented at pH3. Calcium was found to cause droplet aggregation of emulsions made with helianthinin, at neutraland alkaline pH values. Treatments that increase conformational flexibility of the protein moleculeimproved the emulsion properties of sunflower proteins. Keywords: Sunflower; Helianthus annuus; helianthinin; albumin; protein; emulsion; denaturation
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