Collect. Czech. Chem. Commun. 1990, 55, 2110-2117

Oospora lactic lipase: Isolation and properties

Kakhramon Davranov, Mina J. Tabak, Dzhamil Ch. Diyarov, Abdumurod Sattarov and Kamola A. Gulyamova

Institute of Microbiology of Uzbek Academy of Sciences, 700128 Tashkent, U.S.S.R.


Lipase (EC of Oospora lactic UzLM-2 was purified by ammonium sulfate (0.40-0.80) fractionation, gel-filtration on Sephadex G-100, column chromatography on DEAE-Sephadex and CM-Sephadex, gel-filtration on Sephadex G-75 and was finally crystallized in concentrated aqueous solution. Crystalline preparation of the enzyme is homogeneous at disc-electrophoresis and ultracentrifugation. Sedimentation coefficient (S20w) is 3.6 S, isoelectric point (pI) at pH 4.2 and molecular mass of the enzyme is 40-43 kD. Amino acid composition analysis showed that none of sulfur-containing amino acids were detected in the crystalline enzyme, but it contains about 8% of carbohydrates and a small amount of lipids. Lipase from Oospora lactic was most active at pH 7.5 and 37 °C in olive oil, stable in the range of pH from 5.7 to 8.0 at 30-40 °C for 18 h and retained stability at 50 °C for 10 min.