Isolation of a Novel Lipase Gene from Serratia liquefaciens S33 DB-1, Functional Expression in Pichia pastoris and its Properties

文献类型： 外文期刊

第一作者： Yao, Hongyan

作者： Yao, Hongyan;Yu, Shunwu;Zuo, Kaijing;Ling, Hua;Zhang, Fei;Tang, Kexuan;Yu, Shunwu

作者机构：

关键词： Cloning;Expression;Genomic-walking;Lipase;Pichia pastoris;Serratia liquefaciens

期刊名称：MOLECULAR BIOTECHNOLOGY （ 影响因子：2.695； 五年影响因子：2.303 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： A new lipase gene designated as SlLipA was isolated from Serratia liquefaciens S33 DB-1 by the genomic-walking method. The cloned gene contained an open reading frame (ORF) of 1,845 bp encoding 615 amino acids with a conserved GXSXG motif. Genome sequence analysis showed that an aldo/keto reductase gene closed to the SlLipA gene. The lipase gene was cloned into the expression vector pPICZαA and successfully integrated into the heterologous host, methylotrophic yeast Pichia pastoris GS115. Five transformants could be expressed as secreted recombinant proteins with the high activity on Triglyceride–Agarose plate and as candidates to produce the recombinant enzyme. A C-terminal His tag was used for its purification. The lipase activity of different transformants against substrate para-nitrophenyl laurate (p-NPL) varied from 14 to 16 U ml?1. For the substrates para-nitrophenyl caprate (p-NPC), p-NPL, para-nitrophenyl myristate (p-NPM), para-nitrophenyl palmitate (p-NPP), and para-nitrophenyl stearate (p-NPS), the specific activity was shown to be preferred to long acyl chain length of p-NPS.

分类号： Q7

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