Abstract
Abstract Solvent tolerant extracellular lipase from Bacillus sphaericus MTCC 7542 was purified by DEAE–Sepharose anion exchange chromatography. This purification resulted in 377 U/mg specific activity and 17.33-fold with 5.7% recovery obtained. The molecular weight of the purified lipase was determined to be 69 kDa using SDS polyacrylamide gel electrophoresis and conformed by zymogram. The purified lipase showed optimal activity and stability at pH 8.0 and 40 °C. The purified lipase was stable in the presence of hydrophobic solvents like n -butanol, benzene, hexane and toluene. Lipase activity was promoted in the presence of Mg 2+ , Ca 2+ , Cu 2+ , K + and Tween 80.
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