SOLUBILITY AND EMULSIFYING PROPERTIES OF KAPPA CASEIN AND ITS CASEINOMACROPEPTIDE

Abstract

Kappa-casein A was treated with chymosin in order to isolate the caseino-macropeptide corresponding to the C-terminal 106–169 residues of K-casein. Whole casein, K-casein and the caseinomacropeptide (CMP) were studied for their water solubility and emulsifying activity. The CMP was soluble over the range of pH from 1 to 10, with a “minimum” solubility (88%) in the range of pH 1–5 and a “maximum” solubility (98%) in the range of pH 5–10. For whole casein and K-casein, at pH values above 5.5, the emulsifying activity increased when pH increased and the maximum value was obtained for very alkaline solutions; for pH values below 4.5, the increase in emulsifying activity was much more pronounced at pH 2.5; below pH 2.5, emulsifying activity decreased. For CMP, the increase in emulsifying activity was much more pronounced in the acidic range than in the alkaline range. After 24 h storage and heating of the emulsion, a large pH-dependant decrease of emulsifying activity (22–60%) was observed for CMP for pH values below 4.0; under the same conditions, the emulsifying activity of whole casein and K-casein showed a 5–19% and a 1–21% decrease, respectively. For pH values above 6.0, a 22–59% decrease was observed for CMP as compared to a 1–12% and a 4–17% decrease with whole casein and K-casein, respectively.