Degradation of phenol using tyrosinase immobilized on siliceous supports

Abstract

The degradation of phenol by tyrosinase immobilized on chemically modified sodium aluminosilicate (NaA), calcium aluminosilicate (CaA), and silica gel was studied. Phenol conversion by immobilized tyrosinase ranged between approximately 15% and 60%, depending upon the initial phenol concentration, pH, and enzyme loading. Tyrosinase immobilized on CaA and on NaA could be re-used repeatedly without any decrease in performance. However, in studies at pH 8.0, significant enzyme inhibition was observed, since phenol conversion was rapid for approximately 20 min, then reached a plateau. The inhibition was reversible; activity was restored upon placing the immobilized enzyme in fresh substrate. Reducing the pH to 6.8 from 8.0 led to higher conversion of phenol, and decreased the inhibition of the immobilized enzyme.