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SUMMARY: The enzyme endopolygalacturonase secreted by the fungus Ganoderma lucidum was purified by a three-step procedure until pectin methylesterase was no longer detectable. The endopolygalacturonase activity was inhibited by divalent metal ions. The enzyme had a peak of activity at pH 5.4 and two temperature optima: one at 50° and the other at 70°.
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