RT Journal Article SR Electronic(1) A1 Kumari, H. Lalitha A1 Sirsi, M.YR 1971 T1 Purification and Properties of Endopolygalacturonase from Ganoderma lucidum JF Microbiology, VO 65 IS 3 SP 285 OP 290 DO https://doi.org/10.1099/00221287-65-3-285 PB Microbiology Society, SN 1465-2080, AB 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°., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-65-3-285