Abstract
The interaction of β-lactoglobulin (β-1g) with phospholipids in monolayers was studied with a Langmuir film balance. Pressure—area curves of monolayers of β-1g mixed with either egg yolk phosphatidic acid (EYPA) or egg yolk phosphatidylcholine (EYPC) on pH 1.3 to 6 subphases were compared to curves calculated from the results obtained with the individual components. EYPA and β-1g exhibited electrostatic attaction for each other in mixed monlayers at the air—water interface when the pH of the subphase was 4 or 1.3. No interaction was observed on pH 6 subphase. Monolayers of egg yolk phosphatidylcholine-β-1g mixtures exhibited no interaction over the pH range studied. Calcium at 1 m M concentration in the subphase removed the evidence for interaction between EYPA and β-1g at pH 4, but not at pH 1.3. Circular dichroism spectroscopy suggested an increased amount of α helix and β sheet in the films as compared to solutions of β-1g.
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