A novel cold-adapted lipase from Acinetobacter sp XMZ-26: gene cloning and characterisation

文献类型： 外文期刊

第一作者： Zheng, Xiaomei

作者： Zheng, Xiaomei;Chu, Xiaoyu;Zhang, Wei;Wu, Ningfeng;Fan, Yunliu

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关键词： Cold-adapted lipase;Acinetobacter sp.;Detergent additives;Organic synthesis

期刊名称：APPLIED MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：4.813； 五年影响因子：4.697 ）

ISSN： 0175-7598

年卷期： 2011 年 90 卷 3 期

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收录情况： SCI

摘要： Acinetobacter sp. XMZ-26 (ACCC 05422) was isolated from soil samples obtained from glaciers in Xinjiang Province, China. The partial nucleotide sequence of a lipase gene was obtained by touchdown PCR using degenerate primers designed based on the conserved domains of cold-adapted lipases. Subsequently, a complete gene sequence encoding a 317 amino acid polypeptide was identified. Our novel lipase gene, lipA, was overexpressed in Escherichia coli. The recombinant protein (LipA) was purified by Ni-affinity chromatography, and then deeply characterised. The LipA resulted to hydrolyse pNP esters of fatty acids with acyl chain length from C2 to C16, and the preferred substrate was pNP octanoate showing a k (cat) = 560.52 +/- 28.32 s(-1), K (m) = 0.075 +/- 0.008 mM, and a k (cat)/K (m) = 7,377.29 +/- 118.88 s(-1) mM(-1). Maximal LipA activity was observed at a temperature of 15A degrees C and pH 10.0 using pNP decanoate as substrate. That LipA peaked at such a low temperature and remained most activity between 5A degrees C and 35A degrees C indicated that it was a cold-adapted enzyme. Remarkably, this lipase retained much of its activity in the presence of commercial detergents and organic solvents, including Ninol, Triton X-100, methanol, PEG-600, and DMSO. This cold-adapted lipase may find applications in the detergent industry and organic synthesis.

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