Purification and properties of an extracellular lipase from the fungus Botrytis cinerea.
作者： Pascal Comménil , Lionel Belingheri , Michel Sancholle , Bertrand Dehorter
DOI: 10.1007/BF02536044
关键词:
摘要: An extracellular lipase (EC 3.1.1.3) from the fungus Botrytis cinerea has been purified to homogeneity and characterized. The purification included ammonium sulfate fractionation sequential column chromatography. of preparation was 31-fold recovery yield 21%. enzyme associated with esterase activity according staining on polyacrylamide gel. molecular weight determined as 60 kDa sodium dodecyl sulfate-polyacrylamide gel electrophoresis estimated at 72 using filtration, which suggests that may be a monomer. isoelectric point 6.5, optimal obtained 38 degrees C pH 6.0. This showed high specificity for synthetic substrates containing long-chain unsaturated fatty acids umbelliferone esters. effect beta-cyclodextrin hydrolysis olive oil studied. specific 25 mumole/min/mg in absence 132 its presence.
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