A potent lipase from Acinetobacter species

This Monograph describes the impact of a potent lipase producing soil bacterial strain Acinetobacter sp. The characterization of crude lipase from the optimized media showed that lipolytic activity was optimal at pH 8.5 and at 30?C. Lipase activity was stable over a wide pH range [4.0 – 9.5] and significant temperature stability up to 50?C at pH 8.5 was observed. Lipase was stable in commercially available detergents and it was found to be remarkably activated by various salts and also stable in 40%, 80% organic solvents and hydrogen peroxide. Partial purification using 40% ammonium sulphate resulted in an increase in specific activity from 2.34U/mg of protein to 19.23U/mg. Approximate molecular weight for the crude lipase was determined as 32000 Daltons by SDS PAGE analysis. The position of lipase was confirmed by performing SDS PAGE Zymography. The filtered lipase was tested as an additive in laundry detergent formulations using statistical design RSM. Optimization studies showed that an enzyme concentration of 125U, pH 9.5, time of washing of 20 minutes and 0.5% detergent concentration were required for the effective removal of olive oil from cotton fabric.