PROPERTIES OF MUSHROOM AGARICUS BISPORUS TYROSINASE AND IT’S USAGE FOR CHLOROSUBSTITUTED PHENOLS ELIMINATION

Abstract

From mushrooms Agaricus bisporus was isolated partially purified tyrosinase preparation with 3-fold increased specific phenoloxidase activity (13 mcmol purpurogallin/mg of proteinmin, 500 U/mg of proteinmin, respectively, for pyrogallol and tyrosine, with protein yield 0.67mg/ g of mushrooms, copper content 0,19 % , pH-optimum 6,5, thermooptimum 40°C). By the SDS- and native PAGE-electrophoresis method the fractional composition and enzymatic activity of protein fractions in preparation were studied. The isolated enzyme had catalyzed the process of phenol chloroderivatives oxydation with conversion degree of 50-100 %, depending from the substituents number and their position in phenolic nucleus; for the first time the potassium and ammonium alum were used for elimination of the transformation products.

Keywords

• тирозиназа, виділення, властивості, видалення хлорфенолів