1. Purification and biochemical characterization of a novel alkaline (phospho)lipase from a newly isolated Fusarium solani strain.
- Author
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Jallouli R, Khrouf F, Fendri A, Mechichi T, Gargouri Y, and Bezzine S
- Subjects
- Amino Acid Sequence, Bile Acids and Salts pharmacology, Biocatalysis drug effects, Calcium pharmacology, Enzyme Stability, Hydrogen-Ion Concentration, Lactones pharmacology, Orlistat, Phospholipases chemistry, Temperature, Trees microbiology, Wood microbiology, Fusarium enzymology, Fusarium isolation & purification, Phospholipases isolation & purification, Phospholipases metabolism
- Abstract
An extracellular lipase from Fusarium solani strain (F. solani lipase (FSL)) was purified to homogeneity by ammonium sulphate precipitation, gel filtration and anion exchange chromatography. The purified enzyme has a molecular mass of 30 kDa as estimated by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The 12 NH(2)-terminal amino acid residues showed a high degree of homology with a putative lipase from the fungus Necteria heamatoccocae. It is a serine enzyme, like all known lipases from different origins. Interestingly, FSL has not only lipase activity but also a high phospholipase activity which requires the presence of Ca(2+) and bile salts. The specific activities of FSL were about 1,610 and 2,414 U/mg on olive oil emulsion and egg-yolk phosphatidylcholine as substrates, respectively, at pH 8.0 and 37 °C. The (phospho)lipase enzyme was stable in the pH range of 5-10 and at temperatures below 45 °C.
- Published
- 2012
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