Effect of Glycation on the Flocculation Behavior of Protein-Stabilized Oil-in-Water Emulsions

R.J.B.M. Delahaije, H. Gruppen, N.H. van Nieuwenhuijzen, M.L.F. Giuseppin, P.A. Wierenga

Research output: Contribution to journalArticleAcademicpeer-review

22 Citations (Scopus)

Abstract

Glycation of proteins by the Maillard reaction is often considered as a method to prevent flocculation of protein-stabilized oil-in-water emulsions. The effect has been suggested, but not proven, to be the result of steric stabilization, and to depend on the molecular mass of the carbohydrate moiety. To test this, the stabilities of emulsions of patatin glycated to the same extent with different mono- and oligosaccharides (xylose, glucose, maltotriose, and maltopentaose) were compared under different conditions (pH and electrolyte concentration). The emulsions with non-modified patatin flocculate under conditions in which the zeta potential is decreased (around the iso-electric point and at high ionic strength). The attachment of monosaccharides (i.e., glucose) did not affect the flocculation behavior. Attachment of maltotriose and maltopentaose (Mw > 500 Da), on the other hand, provided stability against flocculation at the iso-electric point. Since the zeta potential and the interfacial properties of the emulsion droplets are not affected by the attachment of the carbohydrate moieties, this is attributed to steric stabilization. Experimentally, a critical thickness of the adsorbed layer required for steric stabilization against flocculation was found to be 2.29–3.90 nm. The theoretical determination based on the DLVO interactions with an additional steric interaction coincides with the experimental data. Hence, it can be concluded that the differences in stability against pH-induced flocculation are caused by steric interactions.
Original languageEnglish
Pages (from-to)15201-15208
JournalLangmuir
Volume29
Issue number49
DOIs
Publication statusPublished - 2013

Keywords

  • bovine serum-albumin
  • beta-lactoglobulin
  • physicochemical properties
  • adsorption dynamics
  • disjoining pressure
  • alpha-lactalbumin
  • interfaces
  • particles
  • thickness
  • size

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