• aggregation;
  • β-lactoglobulin;
  • biopolymer particles;
  • core-shell;
  • electrical charge;
  • nanoparticles;
  • pectin;
  • stability

ABSTRACT:  The purpose of this study was to produce and characterize core-shell biopolymer particles based on electrostatic deposition of an anionic polysaccharide (beet pectin) onto amphoteric protein aggregates (heat-denatured β-lactoglobulin [β-lg]). Initially, the optimum conditions for forming stable protein particles were established by thermal treatment (80 °C for 15 min) of 0.5 wt%β-lg solutions at different pH values (3 to 7). After heating, stable submicron-sized (d= 100 to 300 nm) protein aggregates could be formed in the pH range from 5.6 to 6. Core-shell biopolymer particles were formed by mixing a suspension of protein aggregates (formed by heating at pH 5.8) with a beet pectin solution at pH 7 and then adjusting the pH to values where the beet pectin is adsorbed (< pH 6). The impact of pH (3 to 7) and salt concentration (0 to 250 mM NaCl) on the properties of the core-shell biopolymer particles formed was then established. The biopolymer particles were stable to aggregation from pH 4 to 6, but aggregated at lower pH values because they had a relatively small ζ-potential. The biopolymer particles remained intact and stable to aggregation up to 250 mM NaCl at pH 4, indicating that they had good salt stability. The core-shell biopolymer particles prepared in this study may be useful for encapsulation and delivery of bioactive food components or as substitutes for lipid droplets.