Emulsifying Properties of Food Proteins: Bovine Mi cellar Casein

Abstract

ABSTRACT The capacity of micellar casein isolated from bovine milk to stabilize oil in water (0:w) emulsions was studied. Emulsion surface area per unit mass of protein, i.e., emulsifying activity (EA), was highest at a protein concentration of 1% and o:w ratio of 1:9. The surface concentration of micellar casein was related to the o:w ratio being highest at an o:w of 4:6. Interfacial surface area decreased at pH 6.7 reflecting micellar stability and improved with increasing pH apparently because of destabilization of the casein micelle. Emulsion stability was high when the EA was high. The apparent viscosity of the emulsions was inversely related to EA.