文献类型：期刊文献

英文题名：Development of recombinant Escherichia coli whole-cell biocatalyst expressing a novel alkaline lipase-coding gene from Proteus sp. for biodiesel production

作者：Gao, Bei[1]; Su, Erzheng[1]; Lin, Jinping[1]; Jiang, Zhengbing[1]; Ma, Yushu[1]; Wei, Dongzhi[1]

机构：[1] State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai, 200237, China

年份：2009

卷号：139

期号：2

起止页码：169

外文期刊名：Journal of Biotechnology

收录：EI(收录号：20090111829952)

语种：英文

外文关键词：Catalysts - Cloning - Cytology - Gene encoding - Temperature - Biodiesel - Purification - Alkalinity

摘要：A lipase-producing bacterium K107 was isolated from soil samples of China and identified to be a strain of Proteus sp. With genome-walking method, the open reading frame of lipase gene lipK107, encoding 287 amino acids, was cloned and expressed in a heterologous host, Escherichia coli BL21 (DE3). The recombinant lipase was purified and characterized, and the optimum pH of the purified LipK107 was 9, at 35 °C. The recombinant E. coli expressing lipK107 was applied in biodiesel production in the form of whole-cell biocatalyst. Activity of the biocatalyst increased significantly when cells were permeabilized with 0.3% (w/v) cetyl-trimethylammoniumbromide (CTAB). This transesterification was carried out efficiently in a mixture containing 5 M equivalents of methanol to the oil and 100% water by weight of the substrate. It was the first time to use E. coli whole-cell biocatalyst expressing lipase in biodiesel production, and the biodiesel reached a yield of nearly 100% after 12 h reaction at the optimal temperature of 15 °C, which was the lowest temperature among all the known catalyst in biodiesel production. ? 2008 Elsevier B.V. All rights reserved.