Influence of the overall charge and local charge density of pectin on the complex formation between pectin and beta-lactoglobulin

B.L.H.M. Sperber, H.A. Schols, M.A. Cohen Stuart, W. Norde, A.G.J. Voragen

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96 Citations (Scopus)


The complex formation between ß-lactoglobulin (ß-lg) and pectin is studied using pectins with different physicochemical characteristics. Pectin allows for the control of both the overall charge by degree of methyl-esterification as well as local charge density by the degree of blockiness. Varying local charge density, at equal overall charge is a parameter that is not available for synthetic polymers and is of key importance in the complex formation between oppositely charged (bio)polymers. LMP is a pectin with a high overall charge and high local charge density; HMPB and HMPR are pectins with a low overall charge, but a high and low local charge density, respectively. Dynamic light scattering (DLS) titrations identified pHc, the pH where soluble complexes of ß-lg and pectin are formed and pH, the pH of phase separation, both as a function of ionic strength. pHc decreased with increasing ionic strength for all pectins and was used in a theoretical model that showed local charge density of the pectin to control the onset of complex formation. pH passed through a maximum with increasing ionic strength for LMP because of shielding of repulsive interactions between ß-lg molecules bound to LMP, while attractive interactions were repressed at higher ionic strength. Potentiometric titrations of homo-molecular solutions and mixtures of ß-lg and pectin showed charge regulation in ß-lg¿pectin complexes. Around pH 5.5¿5.0 the pKas of ß-lg ionic groups are increased to induce positive charge on the ß-lg molecule; around pH 4.5¿3.5 the pKa values of the pectin ionic groups are lowered to retain negative charge on the pectin. Since pectins with high local charge density form complexes with ß-lg at higher ionic strength than pectins with low local charge density, pectin with a high local charge density is preferred in food systems where complex formation between protein and pectin is desired.
Original languageEnglish
Pages (from-to)765-772
JournalFood Hydrocolloids
Issue number3
Publication statusPublished - 2009


  • bovine serum-albumin
  • whey proteins
  • aqueous-solution
  • acid
  • polyelectrolytes
  • coacervation
  • stabilization
  • conformation
  • carrageenan
  • dependence


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