The thermal stability of three forms of pectin methylesterase purified
from tomato was evaluated at pH 4.5. The time-dependent heat-inactiva
tion curves for the three forms exhibit exponential behaviour in the t
emperature range between 70 degrees C and 90 degrees C. The determinat
ion of D-T and Z parameters displays a different heat-inactivation kin
etic among the three isoenzymes. In particular, two forms (PME(1) and
PME(3)) show similar behaviour with a Z value of 24 degrees C, whereas
the third form (PME(2)) shows a Z value of 15 degrees C.