A Comparison of the Functional and Interfacial Properties of beta-Casein and Dephosphorylated beta-Casein
The functional and interfacial properties of beta-casein and dephosphorylated beta-casein (DeP beta-casein) were studied at pH 7.0 in 10 mM phosphate buffer. A decrease in emulsion stability and an increase in foamability was observed. Results from a variety of interfacial techniques including electrophoretic mobility, thin film thickness, surface and interfacial tension, surface rheology, adsorbed layer thickness, and adsorption isotherms of dephosphorylated beta-casein and beta-casein are reported. The results demonstrate that the phosphorylated groups of the N-terminal region of beta-casein are important for stabilizing emulsions. This is either as a direct result of charge repulsion between beta-casein N-terminal regions or more probably as an indirect result of the reduced N-terminal charge permitting DeP beta-casein to adopt a different interfacial conformation resulting in a loss or reduction of a steric barrier. Copyright 1997 Academic Press. Copyright 1997Academic Press
Husband
FA
Food Biophysics Department, Institute of Food Research, Norwich Laboratory, Norwich Research Park, Colney Lane, Norwich, NR4 7UA, United Kingdom
Wilde
PJ
Mackie
AR
Garrood
MJ