Abstract
Thermal stability of bovine α-lactalbumin in the presence of three different calcium concentrations in aqueous solutions of several concentrations of erythritol, xylitol, sorbitol, and inositol at pH 6.5 was evaluated by UV absorbance, fluorescence spectroscopy, and circular dichroism spectroscopy. At the selected conditions, the thermal denaturation process is reversible and is well described by a two-state model. Results show a higher stability for the holo form of the protein in the presence of calcium, followed by the holo- and the apo-lactalbumin, respectively. The stabilizing effect of the polyols increases with polyol concentration and it is higher for the apo-lactalbumin than holo-lactalbumin and is very small for the protein in the presence of a calcium excess.
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