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Structural changes of α-lactalbumin (α-lac) in response to pH, ionic strength, sugars, and heat treatment were investigated by differential scanning calorimetry (DSC) and Fourier transform infrared (FTIR) spectroscopy. From DSC, two reversible transitions at 39.6 °C (A) and 64.8 °C (B) were observed when α-lac was heated. At pH 3, transition A was partially reversible (14%) while transition B was completely reversible. At pH 9, both transitions were completely irreversible. Heating α-lac at pH 3 resulted in aggregation with no observed gelation; at pH 9 a translucent gel was formed. FTIR showed that at pH 3, denaturation of α-lac resulted in the appearance of two bands at 1616 and 1685 cm - 1 attributed to intermolecular aggregation. These bands were absent at alkaline pH. The major effects of heat treatment of α-lac were loss in the bands attributed to α-helix, 3 10 -helix, and β-sheet and increase in the bands attributed to turns.
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Boye et al. (1997) studied this question.
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