Micrometer-Sized Fibrillar Protein Aggregates from Soy Glycinin and Soy Protein Isolate

C. Akkermans, A.J. van der Goot, P. Venema, H. Gruppen, J.M. Vereijken, E. van der Linden, R.M. Boom

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121 Citations (Scopus)


Long, fibrillar semiflexible aggregates were formed from soy glycinin and soy protein isolate (SPI) when heated at 85 °C and pH 2. Transmission electron microscopy analysis showed that the contour length of the fibrils was ~1 µm, the persistence length 2.3 µm, and the thickness a few nanometers. Fibrils formed from SPI were more branched than the fibrils of soy glycinin. Binding of the fluorescent dye Thioflavin T to the fibrils showed that ß-sheets were present in the fibrils. The presence of the fibrils resulted in an increase in viscosity and shear thinning behavior. Flow-induced birefringence measurements showed that the behavior of the fibrils under flow can be described by scaling relations derived for rodlike macromolecules. The fibril formation could be influenced by the protein concentration and heating time. Most properties of soy glycinin fibrils are comparable to ß-lactoglobulin fibrils.
Original languageEnglish
Pages (from-to)9877-9882
JournalJournal of Agricultural and Food Chemistry
Issue number24
Publication statusPublished - 2007


  • beta-lactoglobulin gels
  • amyloid fibrils
  • globular-proteins
  • thioflavin-t
  • gelation
  • ph
  • denaturation


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