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- W2321480913 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 in- creasing enzyme specific activities in the following or- der: homogenate < sediment at 13 000 g for 30 min < acetone powder < fraction obtained by gel per- meation chromatography. The molecular mass of the enzyme was estimated to be 30 kDa as determined by gel filtration column chromatography." @default.
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- W2321480913 date "1997-07-01" @default.
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- W2321480913 title "Partial purification and characterization of a lipolytic enzyme from spores of the arbuscular mycorrhizal fungus Glomus versiforme" @default.
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- W2321480913 doi "https://doi.org/10.1080/00275514.1997.12026826" @default.
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