Conformational states of sunflower (Helianthus annuus) Helianthinin: Effect of heat and pH.

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

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The structure and solubility of helianthinin, the most abundant protein of sunflower seeds, was investigated as a function of pH and temperature. Dissociation of the 11S form (hexamer) into the 7S form (trimer) gradually increased with increasing pH from 5.8 to 9.0. High ionic strength (I = 250 mM) stabilizes the 11S form at pH > 7.0. Heating and low pH resulted in dissociation into the monomeric constituents (2-3S). Next, the 7S and 11S forms of helianthinin were isolated and shown to differ in their secondary and tertiary structure, and to have denaturation temperatures (Td) of 65 and 90 C, respectively. Furthermore, the existence of two populations of the monomeric form of helianthinin with denaturation temperatures of 65 and 90 C was described. This leads to the hypothesis that helianthinin can adopt two different conformational states: one with Td = 65 C and a second with Td = 90 C.
Original languageEnglish
Pages (from-to)6770-6778
JournalJournal of Agricultural and Food Chemistry
Issue number22
Publication statusPublished - 2004


  • differential scanning calorimetry
  • seed storage proteins
  • physicochemical properties
  • circular-dichroism
  • globulin fraction
  • ionic-strength
  • charge heterogeneity
  • molecular-structure
  • 11-s globulins
  • soy glycinin


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