Solubility and emulsifying properties of kappa casein and its caseinomacropeptide

Autor: Michèle Dalgalarrondo, Catherine Bertrand-Harb, Jean-Marc Chobert, Marie-Georgette Nicolas, A. Touati
Přispěvatelé: Laboratoire d'étude des interactions des molécules alimentaires, Institut National de la Recherche Agronomique (INRA)
Jazyk: angličtina
Rok vydání: 1989
Předmět:
Zdroj: Journal of Food Biochemistry
Journal of Food Biochemistry, Wiley, 1989, 13 (6), pp.457-473
Journal of Food Biochemistry 6 (13), 457-473. (1989)
ISSN: 0145-8884
1745-4514
Popis: 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.
Databáze: OpenAIRE