Partial purification and characterization of a lipolytic enzyme from spores of the arbuscular mycorrhizal fungus Glomus versiforme

Abstract

The lypolytic activity of extracts from G. versiforme spores was detected and measured in in vitro assays using triolein as a substrate. Among the different subcellular fractions assayed, a membrane-rich one showed the greatest lipolytic activity. Like other membrane-bound enzymes, G. versiforme lipase was well extracted in presence of detergent. The time-course of triolein hydrolysis by several lipase preparations was studied. The partial purification of the lipase from the total homogenate 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 mass of the enzyme was estimated to be 30 kDa as determined by gel filtration column chromatography.

Key Words:

• acetone powder
• lipase activity
• spore homogenates
• triacylglycerol hydrolysis