Active laccase and LiP fractions purified from Phanerochaete chrysosporium broth cultures designed for degradation of phenols in sewage samples were immobilized by entrapping in Sol-Gel matrix of trimethoxysilane (TMOS) and propyltetramethoxysilane (PTMS). A maximum of 90.7% and 92.3% of immobilization efficiencies were achieved with a 2 mg/mL pure laccase and pure LiP each. Immobilized laccase and LiP retained 80% and 84% of their activities at pH 4.5 and 5.5 respectively compared to free enzymes. The capacity of the enzyme laccase to withstand the effect of inhibitors (cystein, EDTA, and Ag+) was also enhanced by up to 80% by immobilization. Immobilized Laccase was active in the reaction mixture for three hours, but degraded only 45% of the phenol in one hour whereas immobilized LiP which remained active for one and half hour degraded 95% of phenol in the stipulated one hour time. When immobilized laccase was treated with divalent metal ions Ca++ and Cu++ it worked faster equal to immobilized LiP and degraded 96% phenol in one hour and remained active for 3 hours.
Keywords: Phanerochaete chrysosporium,Laccase,Lignin Peroxidase,Manganese Peroxidase,
Purification and Enzyme Immobilization.