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Both proteins are able to bind seve rai cations at pH 6.6 when ionie strength is low. The affinity of o-lactalbumin for the first bound atom is high, then decreases for the following ions. In these physico-chemical conditions of the aqueous phase (pH 6.6 fL < 0.01), the maximal number of bound cations depends on the mineraI. The binding ability of œ-lactalbumin is 3.0 ions of Mn2+, 3.5 of Mg2+, 4.5 of Ca2+ and Zn2+, 6.0 of Fe2+, 10.6 of Cu2+ and more than 2.0 ions of Mn2+, 2.5 of Zn2+, 3.2 of Mg2+ and 3.5 of Ca2+, Fe2+, Cu2+ for 13-lactoglobulin. The affinity of o-lactalbumin is high for Ca2+, Zn2+, Mn2+, Cu2+ and reduced for Mg2+ and Fe+. For Jj-Iactoglobulin the affinity is high for Zn2+, Fe2+, Cu2+, and lower for Ca2+, Mg2+ and Mn2+.

Binding of bivalent cations to α-lactalbumin and β-lactoglobulin: effect of pH and ionic strength