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- Title
Purification and Biochemical Characterization of a Novel Alkaline (Phospho)lipase from a Newly Isolated Fusarium solani Strain.
- Authors
Jallouli, Raida; Khrouf, Fatma; Fendri, Ahmed; Mechichi, Tahar; Gargouri, Youssef; Bezzine, Sofiane
- 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 NH2- 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 Ca2+ 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.
- Subjects
FUSARIUM solani; ORLISTAT; ION exchange chromatography; LECITHIN; HOMOGENEITY; POLYACRYLAMIDE gel electrophoresis
- Publication
Applied Biochemistry & Biotechnology, 2012, Vol 168, Issue 8, p2330
- ISSN
0273-2289
- Publication type
Article
- DOI
10.1007/s12010-012-9940-0