Mesostructure of fibrillar bovine serum albumin gels

C. Veerman, J. Heck, L.M.C. Sagis, E. van der Linden

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80 Citations (Scopus)

Abstract

The mesostructure of bovine serum albumin (BSA) at low pH was investigated. Rheological measurements were performed to determine the critical percolation concentration (cp). A decreasing cp with increasing ionic strength was found. Fibrils with a contour length of about 100–300 nm were found using transmission electron microscopy. The measured conversion of monomers into fibrils was independent of ionic strength (0.20–0.30 M). Dilution of BSA samples showed that the aggregation process is reversible and that there exists a critical concentration for the self-assembly of BSA. We explain the decreasing cp with increasing ionic strength in terms of an adjusted random contact model.
Original languageEnglish
Pages (from-to)139-146
JournalInternational Journal of Biological Macromolecules
Volume31
Issue number4-5
DOIs
Publication statusPublished - 2003

Keywords

  • heat-induced gelation
  • protein gels
  • beta-lactoglobulin
  • globular-proteins
  • ionic-strength
  • ph
  • percolation

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