Impact of cosolvents on formation and properties of biopolymer nanoparticles formed by heat treatment of b-lactoglobulin-Pectin complexes

The purpose of this study was to determine the influence of neutral cosolvents on the formation and properties of biopolymer nanoparticles formed by thermal treatment of protein-polysaccharide electrostatic complexes. Biopolymer particles were formed by heating (85 C, 20 min) an aqueous solution containing a globular protein (b-lactoglobulin) and an anionic polysaccharide (beet pectin) above the thermal denaturation temperature (T(m)) of the protein under pH conditions where the biopolymers formed electrostatic complexes (pH 5). The impact of two neutral cosolvents (glycerol and sorbitol) on the self- association of b-lactoglobulin and on the formation of b-lactoglobulin-pectin complexes was examined as a function of solution pH (3-7) and temperature (30-95 C). Glycerol had little impact on the pH-induced self-association or aggregation of the biopolymers, but it did increase the thermal aggregation temperature (T(a)) of the protein-polysaccharide complexes, which was attributed to its ability to increase aqueous phase viscosity. Sorbitol decreased the pH where insoluble protein-polysaccharide complexes were formed, and greatly increased their T(a), which was attributed to its ability to increase T(m), alter biopolymer-biopolymer interactions, and increase aqueous phase viscosity. This study shows that neutral cosolvents can be used to modulate the properties of biopolymer nanoparticles prepared by thermal treatment of protein-polysaccharide electrostatic complexes.