Optimization of cold-active lipase production by CALIP1 from deep-sea sediment-derived metagenomic library

A clone, CALIP1, exhibiting lipase activity was selected from the metagenomic library derived from deep-sea sediment. The purified lipase displayed optimal activity at pH 8.0 and 25 degrees C and maximal stability at 30 degrees C, indicating that the lipase from CALIP1 is a cold-active enzyme. To enhance the lipase production, the Plackett-Burman design was selected to screen the medium components that significantly influence the production. Three components that influenced the production include olive oil, yeast extract powder and (NH4)(2)SO4. The optimal concentration of these components was determined by response surface methodology which is based on the central composite design. Under the proposed optimized conditions, the lipase experimental yield (2760 Uml(-1)) closely matched the predicted yield by the statistical model (2811.84 Uml(-1)) with R-2 = 0.987. An overall 86.5% increase in lipase yield compared with the original culture medium.