Abstract
Tyrosinase is a copper-containing enzyme present in plant and animal tissues, which catalyzes the production of melanin and other pigments. In organic solvent, tyrosinase can convert N-acetyl-l-tyrosine ethyl ester (insoluble in aqueous) to a derivative of l-dopamine (a drug used for the treatment of Parkinson's disease). Thus, the performances of tyrosinase in organic solvent have attracted scientific attention since 1980. In this work, we investigated the stability of immobilized tyrosinase at high temperature in anhydrous organic solvent. Triethylaminoethyl cellulose (TEAE-Cellulose) performed the best out of six immobilization platforms. The dry immobilized tyrosinase became extremely thermostable in organic solvent, and the half-life of the dry immobilized tyrosinase in organic solvent is strongly related to the polarity of the organic solvent than their log P value. The immobilized tyrosinase loses its activity instantaneously in aqueous solution at 100 °C, but it keeps enzymatic activity within 10 min in hydrophilic methanol and over one month in hydrophobic hexane (log P: 4.66, non-polar) even incubating at 100 °C. This research provides valuable information for the design of new biocatalysts.