Notice of RetractionProduction, Purification and Characterization of Lipase from Serratia sp.SL-11

Abstract

[Objective]: To purified and studied the characterization of alkaline lipase. [Methods]: Lipases were isolated from Serratia sp.SL-11 bacterial fermentation broth by centrifugation, ultrafiltration, ion exchange, gel filtration. [Results]: Their specific activity was 6690.1U/mg protein and 5770.50U/mg protein, the purification fold was 35.08 and 40.67, the molecular weight was 319KD and 377KD, respectively. The purity of the purified lipases was confirmed by the presence of a single band on SDS-PAGE. The optimum pH and temperature of SLP-1 is 9.0 and 50°C respectively. The optimum pH and temperature of SLP-2 is 9.0 and 47°C. [Conclusion]: The two enzymes have a strong thermal stability, and have some of the alkali-resistant. They are suitable for industrial application.