IMMOBILIZATION AS A TOOL FOR THE STABILIZATION OF LIGNIN PEROXIDASE PRODUCED BY PHANEROCHAETE-CHRYSOSPORIUM INA-12

Lignin peroxidase immobilization was achieved by covalent coupling on CNBr-Sepharose 4B. Protein immobilization yield was around 80%. For ve ratryl alcohol oxidation, in the presence of hydrogen peroxide, both s oluble and bound enzymes exhibited the same pH profile with an optimum near 2.5. Catalytic parameters (kc and K(m)) were seriously affected by immobilization. On the other hand, immobilization provided a notice able stabilization of the enzyme against acidic pH and high temperatur es. A 15-20 increase in the half-inactivation times at pH 2.2 and 2.7, respectively, could be observed. Bound enzyme was also much more ther mostable than soluble.