Core-Shell Biopolymer Nanoparticles Produced by Electrostatic Deposition of Beet Pectin onto Heat-Denatured Beta-Lactoglobulin Aggregates

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 beta-lactoglobulin [beta-lg]). Initially, the optimum conditions for forming stable protein particles were established by thermal treatment (80 degrees C for 15 min) of 0.5 wt% beta-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 (\u3c 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 -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

Fabrication and morphological characterization of Biopolymer particles formed by electrostatic complexation of heat treated Lactoferrin and Anionic Polysaccharides

Biopolymer particles fabricated from proteins and/or polysaccharides can be used to encapsulate functional components or to modify various functional properties of materials. In this study, sub-micrometer biopolymer particles were fabricated by electrostatic complexation of heat-denatured protein (lactoferrin, LF) particles with anionic polysaccharides (alginate, carrageenan, or pectin). The aim of the study was to exploit macromolecular electrostatic interactions to form sub-micrometer sized particles and study their stability and morphological characteristics. Initially, protein particles were formed by heat treatment (91 °C, 20 min) of a lactoferrin solution (0.2% LF, pH 7), which led to a suspension of protein particles with mean diameter of 200−400 nm and isoelectric point of pI ≈ 8.5. Biopolymer particles were then formed by mixing the protein particles with anionic polysaccharides at pH 8 and then lowering the pH to promote electrostatic deposition of polysaccharides onto the protein particle surfaces. The influence of pH (2−11) and ionic strength (0−200 mM NaCl) on the properties and stability of the complexes was studied using turbidity, dynamic light scattering, and electrophoresis measurements. Relatively stable particles could be formed from pH 5 to 8, but appreciable aggregation occurred at lower pH which was attributed to charge neutralization and bridging effects. LF−pectin complexes were relatively stable to salt addition, but LF−carrageenan and LF−alginate complexes exhibited aggregation at higher salt concentrations. These results have important implications for the application of lactoferrin−polysaccharide complexes as functional components in commercial products, such as pharmaceuticals, personal care products, and foods