Emulsion properties of sunflower (Helianthus annuus) proteins

S. Gonzalez-Perez, G.A. van Koningsveld, J.M. Vereijken, K.B. Merck, H. Gruppen, A.G.J. Voragen

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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 after heat treatment of the proteins. The emulsions were characterized with respect to average droplet size, surface excess, and the occurrence of coalescence and/or droplet aggregation. Sunflower proteins were shown to form stable emulsions, with the exception of SFAs at neutral and alkaline pH values. Droplet aggregation occurred in emulsions made with SI, helianthinin, and SFAs. Droplet aggregation and subsequent coalescence of emulsions made with SFAs could be prevented at pH 3. Calcium was found to cause droplet aggregation of emulsions made with helianthinin, at neutral and alkaline pH values. Treatments that increase conformational flexibility of the protein molecule improved the emulsion properties of sunflower proteins.
Original languageEnglish
Pages (from-to)2261-2267
JournalJournal of Agricultural and Food Chemistry
Issue number6
Publication statusPublished - 2005


  • seed storage proteins
  • functional-properties
  • physicochemical properties
  • emulsifying properties
  • charge heterogeneity
  • globulin fraction
  • chlorogenic acid
  • soy proteins
  • albumin
  • meal

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    Gonzalez-Perez, S., van Koningsveld, G. A., Vereijken, J. M., Merck, K. B., Gruppen, H., & Voragen, A. G. J. (2005). Emulsion properties of sunflower (Helianthus annuus) proteins. Journal of Agricultural and Food Chemistry, 53(6), 2261-2267. https://doi.org/10.1021/jf0486388