Li Jianrong, Deng Yu, Jing Haiming, Cheng Lili, Zhao Xin, Tang Yun-ming
{"title":"Notice of RetractionProduction, Purification and Characterization of Lipase from Serratia sp.SL-11","authors":"Li Jianrong, Deng Yu, Jing Haiming, Cheng Lili, Zhao Xin, Tang Yun-ming","doi":"10.1109/ICBBE.2011.5780013","DOIUrl":null,"url":null,"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.","PeriodicalId":6438,"journal":{"name":"2011 5th International Conference on Bioinformatics and Biomedical Engineering","volume":"24 1","pages":"1-4"},"PeriodicalIF":0.0000,"publicationDate":"2011-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"2011 5th International Conference on Bioinformatics and Biomedical Engineering","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/ICBBE.2011.5780013","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1
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.
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