Purification and Properties of Endopolygalacturonase from Ganoderma lucidum

H. LALITHA KUMARI; M. SIRSI

doi:10.1099/00221287-65-3-285

Purification and Properties of Endopolygalacturonase from Ganoderma lucidum

H. LALITHA KUMARI and M. SIRSI
First Published: 01 March 1971 https://doi.org/10.1099/00221287-65-3-285

Abstract

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°.

Accepted: 01/01/1971
Published Online: 01/03/1971

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Microbiology

Volume 65, Issue 3

Research Article

Free

Purification and Properties of Endopolygalacturonase from Ganoderma lucidum

Abstract

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