| Summary: | Polyphenol oxidase (PPO) was purified and characterized from a dried wild edible and medicinal mushroom (<i>V</i>. <i>bombycina</i>). Using Sepharose 4B-L-tyrosine-<i>p</i>-aminobenzoic acid affinity chromatography, PPO was purified from the dried <i>V</i>. <i>bombycina.</i> 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 (<i>Km</i> and <i>Vmax</i>). At the optimum pH and temperature, dried <i>V</i>. <i>bombycina</i> PPO’s <i>Km</i> and <i>Vmax</i> 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 <i>V</i>. <i>bombycina</i>. The optimum pH and temperature values for dried <i>V</i>. <i>bombycina</i> 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 <i>V</i>. <i>bombycina</i>.
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