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Emulsifying Properties of Food Proteins: Bovine Mi cellar Casein
Author(s) -
HAQUE ZAHURUL,
LEMAN JACEK,
KINSELLA JOHN E.
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb13540.x
Subject(s) - emulsion , chemistry , casein , micelle , chromatography , viscosity , bovine milk , food science , aqueous solution , biochemistry , organic chemistry , materials science , composite material
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.