PARTIAL-PURIFICATION AND CHARACTERIZATION OF A LIPOLYTIC ENZYME FROM SPORES OF THE ARBUSCULAR MYCORRHIZAL FUNGUS GLOMUS VERSIFORME

The lypolytic activity of extracts from G. versiforme spores was detec ted and measured in in vitro assays using triolein as a substrate. Amo ng the different subcellular fractions assayed, a membrane-rich one sh owed the greatest lipolytic activity. Like other membrane-bound enzyme s, G. versiforme lipase was well extracted in presence of detergent. T he time-course of triolein hydrolysis by several lipase preparations w as studied. The partial purification of the lipase from the total homo genate revealed increasing enzyme specific activities in the following order: homogenate < sediment at 13 000 g for 30 min < acetone powder < fraction obtained by gel permeation chromatography The molecular mas s of the enzyme was estimated to be 30 kDa as determined by gel filtra tion column chromatography.