M. Rodriguez et al., STABILITY OF INVERTASE IN ALCOHOLYSIS REACTIONS WITH METHANOL, Journal of molecular catalysis. B, Enzymatic, 2(6), 1997, pp. 299-306
The effect of methanol on the stability and structure of invertase is
reported. It is shown by intrinsic fluorescence, that methanol induces
irreversible changes in structure leading to its deactivation, while
concentrations higher than 20% v/v also lead to aggregation and eventu
al precipitation, a phenomenon which does not involve deactivation. On
the other hand, low concentrations of methanol change the kinetic beh
avior of enzyme as it acts as a mixed type inhibitor.