Production and characterization of two heterologous esterases from Thermus thermophilus in a mesophilic yeast

Abstract

SFurthermore, the apparent kinetic parameters of the reactivated biocatalyst present only a partial recovery of their values before inactivation. By contrast, the reactivation strategy plays an important role resulting in a biocatalyst with different kinetic properties. Intrinsic parameters of the inactivated and reactivated biocatalyst were determined and no significant differences were detected. These results suggest that conformational changes cannot be reverted by a simple reactivation strategy.It has been demonstrated that after inactivation and further reactivation a substantial level of recovery of enzyme activity can be obtained. However, the kinetic behavior of the biocatalyst cannot be reverted. The impact of changes in kinetic parameters should have a significant effect on the design and operation of enzyme reactors.