The stability of invertase was studied under various conditions, inclu
ding at 75 degrees C, in presence of stabilizers (sorbitol and glycero
l) at 75 degrees C, and in the presence of denaturants (urea and trich
loroacetic acid) at 37 degrees C in reverse micelles. Stability of the
invertase in reverse micelles was found to be improved over that of t
he enzyme in bulk aqueous solution. Sorbitol could enhance enzyme stab
ility as it does in the bulk aqueous system. The stabilizing effect of
glycerol was reduced in reverse micelles. The denaturation pattern of
urea remains unaltered. However, the denaturation effect of trichloro
acetic acid has been reduced in reverse micelles.