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Effect of high-methoxy pectin on properties of casein-stabilized emulsions
Authors:Eric Dickinson  Maria G Semenova  Anna S Antipova  Edward G Pelan
Affiliation:aProcter Department of Food Science, University of Leeds, Leeds LS2 9JT, UK;bInstitute of Biochemical Physics, Russian Academy of Sciences, Moscow 117813, Russia;cUnilever Research Laboratorium, Olivier van Noortlaan 120, 3133 AT Vlaardingen, Netherlands
Abstract:We report on the effect of high-methoxy pectin on the stability and rheological properties of fine sunflower oil-in-water emulsions prepared with αs1-casein, β-casein or sodium caseinate. The aqueous phase was buffered at pH 7.0 or 5.5 and the ionic strength was adjusted with sodium chloride in the range 0.01–0.2 M. Average emulsion droplet sizes were found to be slightly larger at the lower pH and/or with pectin present during emulsification. Analysis of the serum phase after centrifugation indicated that some pectin becomes incorporated into the interfacial layer at pH 5.5 but not at pH 7.0. This was also supported by electrophoretic mobility measurements on protein-coated emulsion droplets and surface shear viscometry of adsorbed layers at the planar oil–water interface. A low pectin concentration (0.1 wt%) was found to give rapid serum separation of moderately dilute emulsions (11 vol% oil, 0.6 wt% protein) and highly pseudoplastic rheological behaviour of concentrated emulsions (40 vol% oil, 2 wt% protein). We attribute this to reversible depletion flocculation of protein-coated droplets by non-adsorbed pectin. At ionic strength below 0.1 M, the initial average droplet sizes, the creaming behaviour, and the rheology were found to be similar for emulsions made with either of the individual caseins (αs1 and β) or with sodium caseinate. At higher ionic strength, however, whereas emulsions containing β-casein or sodium caseinate were stable, the corresponding αs1-casein emulsions exhibited irreversible salt-induced flocculation which was not inhibited by the presence of the pectin.
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