PURIFICATION AND CHARACTERIZATION OF SOLVENT STABLE LIPASE FROM A SOLVENT TOLERANT STRAIN OF GEOBACILLUS STEAROTHERMOPHILUS PS 11

Abstract

An extracellular organic solvent stable lipase produced by solvent tolerant strain of Geobacillus stearothermophilus PS11 was purified and characterised. The overall purification was 8.04 fold with a yield of 22.6%. The molecular weight of purified lipase was approximately 27.5 kDa. The purified lipase activity was stable (745 EU/ml at 72h incubation) in presence of toluene, benzene, propanol, methanol etc. The enzyme activity was maximum (764 EU/ml) when assayed under optimum temperature and pH of 50â°C and 10.0, respectively. The enzyme showed stability at a wide range of temperature from 10â°C to 60â°C. This solvent stable lipase can be a novel tool for biodiesel industry.