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A novel psychrophilic lipase from Pseudomonas fluorescens with unique property in chiral resolution and biodiesel production via transesterification  ( EI收录)  

文献类型:期刊文献

英文题名:A novel psychrophilic lipase from Pseudomonas fluorescens with unique property in chiral resolution and biodiesel production via transesterification

作者:Luo, Yu[1]; Zheng, Yitao[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, 130 Meilong Road, 200237 Shanghai, China

年份:2006

卷号:73

期号:2

起止页码:349

外文期刊名:Applied Microbiology and Biotechnology

收录:EI(收录号:20075110985630)

语种:英文

外文关键词:Affinity chromatography - Amino acids - Biodiesel - Catalyst activity - Escherichia coli - Gene expression - Lipases

摘要:A lipase-producing bacterium strain B68 screened from soil samples of China was identified as Pseudomonas fluorescens. With GenomeWalker, the open reading frame of lipase gene lipB68, encoding 476 amino acids, was cloned and expressed in Escherichia coli BL21 (DE3). By affinity chromatography, the recombinant LipB68 protein was purified to the purity of 95%. As a member of lipase subfamily I.3, LipB68 has a unique optimum temperature of 20 °C, which was the lowest in this subfamily. In chiral resolution, LipB68 effectively catalyzed the transesterification of both α-phenylethanol and α- phenylpropanol at 20 °C, achieving E values greater than 100 and 60 after 120 h, respectively. Among all the known catalysts in biodiesel production, LipB68 produced biodiesel with a yield of 92% after 12 h, at the lowest temperature of 20 °C, and is the first one of the I.3 lipase subfamily reported to be capable of catalyzing the transesterification reaction of biodiesel production. Since lipase-mediated biodiesel production is normally carried out at 35-50 °C, the availability of a highly active lipase with a low optimal temperature can provide substantial savings in energy consumption. Thus, this novel psychrophilic lipase (LipB68) may represent a highly competitive energy-saving biocatalyst. ? Springer-Verlag 2006.

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