Effect of electrostatic Interactions on the Percolation Concentration of Fibrillar ß-Lactoglobuline Gels

C. Veerman, H.G.M. Ruis, L.M.C. Sagis, E. van der Linden

Research output: Contribution to journalArticleAcademicpeer-review

118 Citations (Scopus)

Abstract

The effect of electrostatic interactions on the critical percolation concentration (cp) of fibrillar -lactoglobulin gels at pH 2 was investigated using rheological measurements, transmission electron microscopy (TEM), and performing conversion experiments. A decreasing cp with increasing ionic strength was found. The fraction of nonaggregated -lactoglobulin was independent of ionic strength in the regime of 0.01-0.08 M. TEM experiments showed long fibrils (2-7 m) for ionic strengths between 0.01 and 0.08 M. Since both the conversion of monomers and the contour length of the fibrils were independent of ionic strength (0.01-0.08M), the linear increase of cp with the Debye length can be attributed purely to an increase of electrostatic repulsion between the fibrils. This increase is explained in terms of an adjusted random contact model which takes into account the charge and semiflexibility of the fibrils
Original languageEnglish
Pages (from-to)869-873
JournalBiomacromolecules
Volume3
Issue number4
DOIs
Publication statusPublished - 2002

Keywords

  • heat-induced gelation
  • globular-proteins
  • ionic-strength
  • induced aggregation
  • ph
  • denaturation
  • kinetics
  • whey

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