The conformational stability of beta-lactoglobulin increases in D2O ov
er that in H2O. This is concluded from an increase in peak temperature
by about 3 degrees C of differential scanning calorimetry (DSC) therm
ograms and from a decrease in overall aggregation rate. However, effec
ts of pH and salt concentration on the heat-induced aggregation (react
ion kinetics, DSC thermograms and aggregate growth) are similar in H2O
and D2O. This indicates that the mechanism of heat-induced aggregatio
n of beta-lactoglobulin is not significantly affected by replacement o
f H2O with D2O. (C) 1998 Federation of European Biochemical Societies.