The reversible folding-unfolding transition of mature and precursor fo
rms of Bacillus subtilis levansucrase were compared under physiologica
l conditions of pH and temperature. The time constant of the folding r
eaction was not modified by the presence of the signal sequence and th
e precursor in the native form was slightly more resistant to the dena
turing action of urea. However, the folding pathway could be different
for each protein since a domain of the mature levansucrase underwent
an independent transition which is not observed during the renaturatio
n process of prelevansucrase.