@article{mbs:/content/journal/micro/10.1099/00221287-65-3-285, author = "Kumari, H. Lalitha and Sirsi, M.", title = "Purification and Properties of Endopolygalacturonase from Ganoderma lucidum", journal= "Microbiology", year = "1971", volume = "65", number = "3", pages = "285-290", doi = "https://doi.org/10.1099/00221287-65-3-285", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-65-3-285", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", 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°.", }