Abstract
The conformational stability of β-lactoglobulin increases in D 2O over that in H 2O. This is concluded from an increase in peak temperature by about 3°C of differential scanning calorimetry (DSC) thermograms and from a decrease in overall aggregation rate. However, effects of pH and salt concentration on the heat-induced aggregation (reaction kinetics, DSC thermograms and aggregate growth) are similar in H 2O and D 2O. This indicates that the mechanism of heat-induced aggregation of β-lactoglobulin is not significantly affected by replacement of H 2O with D 2O.
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