An extracellular lipase was isolated and purified from a bacterium and is the first report on the isolation and purification of lipase from the species B. pumilus. Effect of temperature, pH and composition of culture medium were optimized for maximum lipase production. The enzyme was purified and the purity was found to be 98%. The Km value of the enzyme was 1.75 x 10-2 mg. and it was found to be a monomer by SDS PAGE. This lipase was found to be alkaline and thermostable and was not a metalloprotein as evidenced from EDTA treatment. Immobilized whole cells were found to be more stable than the pure enzyme.
|Original language||English (US)|
|Number of pages||5|
|Journal||Indian Journal of Experimental Biology|
|State||Published - Dec 1 1999|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology