Coacervate formation of α-lactalbumin–chitosan and β-lactoglobulin–chitosan complexes

Abstract

α-Lactalbumin (α-La) and β-lactoglobulin (β-Lg) are important whey proteins with isoelectric points of pH 4.80 and 5.34, respectively, and evidence negative charge over a range of pHs. Chitosan exhibits a cationic property under pH 6.5. In an effort to determine the physicochemical properties of mixtures of 0.5% α-La and 0.1% chitosan, and 0.5% β-Lg and 0.1% chitosan, optical structure, turbidity, electrophoresis, differential scanning calorimetry (DSC) and scanning electron microscopy (SEM) were assessed in a pH range of 2.0–8.0. The results demonstrated that α-La, β-Lg, and chitosan precipitated at pH values of approximately 5.0, 5.0, and 7.0, respectively. The mixtures of α-La and chitosan as well as β-Lg and chitosan coacervated at a pH range of 6.0–6.5. The turbidity of α-La and α-La–chitosan achieved a maximum at pH 5.0, whereas those of β-Lg and β-Lg–chitosan achieved maximum values at a pH of 6.5. The electrophoregram showed a large band with high molecular weight in increasing pH values from 5.0 to 6.0, which suggested that α-La and β-Lg form polymers with chitosan. The denaturation temperature and enthalpy of α-La were shown to increase, whereas those of β-Lg were reduced. The SEM images demonstrated that the α-La was characterized by uneven and associated cluster morphology, whereas that of β-Lg was even, globular, and harbored dense particles, whereas the chitosan evidenced a flat morphology. Our assessment of the complex demonstrated that α-La and β-Lg attached to the surface of the chitosan. The α-La–chitosan and β-Lg–chitosan complexes evidenced opposite charges at a pH range of 5.0–6.0, and formed coacervates. It appears, therefore, that the α-La–chitosan and β-Lg–chitosan coacervates might be applied as a delivery system for foods, nutraceuticals, cosmetics, and drugs.