Abstract
The adsorption isotherms of α s-, β- and κ-caseins and a Na-caseinate on polystyrene lattices (10% w/w aqueous suspension) were measured. Adsorption plateaus for α s- and κ-caScins and a Na-caseinate were observed at protein concentrations of about one-half of that required for the plateau of the β-casein adsorption isotherm. Surface tension and free protein measurements showed a strong adsorption of the caseins on the lattices at protein concentrations below a range of 15–20 mg/g of polystyrene lattices. At higher protein concentrations a weaker adsorption of the caseins was observed. Viscosities of polystyrene/protein suspensions gradually increased to a maximum as the protein concentration was increased to ~20 mg/g of polystyrene lattices. This is thought to be caused by flocculation resulting from protein bridging of the polystyrene particles. The viscosities of the polystyrene/κ-casein suspensions were higher than the other three polystyrene/protein suspensions probably because κ-casein is less effective as a steric stabilizer. The maximum viscosity of polystyrene/β-casein suspensions occurred at a ratio of β-casein to polystyrene of ~2%.
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