Title :
Notice of Retraction
Production, Purification and Characterization of Lipase from Serratia sp.SL-11
Author :
Liang Jianrong ; Deng Yu ; Jing Haiming ; Cheng Lili ; Zhao Xin ; Tang Yunming
Author_Institution :
Key Lab. of Eco-environments in Three Gorges Reservoir Region Minist. of Educ., Southwest Univ., Chongqing, China
Abstract :
Notice of Retraction
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
[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.
Keywords :
centrifuges; chemical engineering; ion exchange; purification; thermal stability; ultrafiltration; SDS-PAGE; Serratia sp SL-11; alkali resistant; alkaline lipase characterization; bacterial fermentation; centrifugation; gel filtration; ion exchange; lipase; molecular weight; optimum pH; optimum temperature; protein; purification; purification fold; purified lipase; temperature 50 degC; thermal stability; ultrafiltration; Materials; Microorganisms; Presses; Proteins; Purification; Thermal stability;
Conference_Titel :
Bioinformatics and Biomedical Engineering, (iCBBE) 2011 5th International Conference on
Conference_Location :
Wuhan
Print_ISBN :
978-1-4244-5088-6
DOI :
10.1109/icbbe.2011.5780013
