Emulsion and foam properties of plasmin derived β-casein peptides

Abstract

In the present study the influence of plasmin hydrolysis of β -casein ( β CN) on the foam and emulsion properties was tested. The hydrophilic, amphipathic and hydrophobic fractions produced by plasmin hydrolysis of β CN and fractionation of the hydrolysate, show clear differences in emulsion, foam and surface-active properties. The hydrophilic peptide possessed poor functional properties. The hydrophobic peptides from β CN showed interesting foam properties, especially at acidic pH. The amphipathic peptides exhibited improved emulsion-forming properties, compared to intact β CN. It seemed that the presence of the hydrophilic N-terminus (i.e. fragment 1–28) in these amphipathic peptides was important for their stabilising properties.