Purification and Properties of Polyphenol Oxidase of Dried .

Polyphenol oxidase (PPO) was purified and characterized from a dried wild edible and medicinal mushroom (. ). Using Sepharose 4B-L-tyrosine--aminobenzoic acid affinity chromatography, PPO was purified from the dried . The purification was completed with a 33.85-fold purification. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the purified enzyme migrated as a single band. The molecular weight of the purified enzyme was estimated by SDS-PAGE to be about 25 kDa. Catechol, 4-methyl catechol, and pyrogallol were used as substrates to determine the enzyme activity and its kinetic parameters ( and ). At the optimum pH and temperature, dried . PPO's and values for catechol, 4-methyl catechol, and pyrogallol were found to be 1.67 mM-833.33 U/mL, 3.17 mM-158.73 U/mL, and 2.67 mM-3333.33 U/mL, respectively. Also investigated were the effects of pH and temperature on the enzymatic properties of PPO in dried . . The optimum pH and temperature values for dried . PPO obtained by using catechol, 4-methyl catechol, and pyrogallol as substrates were 6.5, 15 °C; 9.0, 20 °C; and 8.0, 15°C, respectively. This is the first study on the purification and characterization of PPO from dried . .