Effects of heat on physicochemical properties of whey protein-stabilised emulsions

E.L. Sliwinski, F.D. Zoet, M.A.J.S. van Boekel, J.T.M. Wouters, P.J. Roubos-van den Hil

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62 Citations (Scopus)


The effect of heating has been studied for whey protein-stabilised oil-in-water emulsions (25.0% (w/w) soybean oil, 3.0% (w/w) whey protein isolate, pH 7.0). These emulsions were heated between 55 and 95 degreesC as a function of time and the effect on particle size distribution, adsorbed protein amount, protein conformation and rheological properties was determined. Heating the emulsions as a function of temperature for 25 min resulted in an increase of the mean diameter (d(32)) and shear viscosity with a maximum at 75 degreesC. Heating of the emulsions at different temperatures as a function of time in all cases resulted in a curve with a maximum for d(32). A maximum increase of d(32) was observed after about 45 min at 75 degreesC and after 6-8 min at 90 degreesC. Similar trends were observed with viscosity measurements. Confocal scanning laser micrographs showed that after 8 min of heating at 90 degreesC large, loose aggregates of oil droplets were formed, while after 20 min of heating compact aggregates of two or three emulsion droplets remained. An increase of the adsorbed amount of protein was found with increasing heating temperature. Plateau values were reached after 10 min of heating at 75 degreesC and after 5 min of heating at 90 degreesC. Based on these results we concluded that in the whole process of aggregation of whey protein-stabilised emulsions an essential role is played by the non-adsorbed protein fraction, that the kinetics of the aggregation of whey protein-stabilised emulsions follow similar trends as those for heated whey protein solutions and that upon prolonged heating rearrangements take place leading to deaggregation of initially formed large, loose aggregates of emulsion droplets into smaller, more compact ones. (C) 2003 Elsevier B.V. All rights reserved.
Original languageEnglish
Pages (from-to)231-242
Number of pages12
JournalColloids and Surfaces. B: Biointerfaces
Publication statusPublished - 2003


  • beta-lactoglobulin
  • adsorbed proteins
  • globular-proteins
  • ionic-strength
  • denaturation
  • kinetics
  • milk
  • conformation
  • aggregation
  • adsorption

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