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Cloning and Expression of Pseudomonas fluorescens 26-2 Lipase Gene in Pichia pastoris and Characterizing for Transesterification

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Abstract

Pseudomonas lipases are important biocatalysts widely used in a variety of industrial fields. An extracellular lipase gene lipA with 1,854-bp open reading frame was cloned from Pseudomonas fluorescens 26-2. The multialignment assay of the putative amino acid and the secondary structure prediction revealed this enzyme could be classified into the lipolytic subfamily I.3 and secreted via adenosine-triphosphate-binding cassette pathway. The lipA gene was integrated into Pichia pastoris GS115, and the methanol-inducible recombinants with MutS and Mut+ phenotypes were acquired. The characteristics and the transesterification capacity shown by this enzyme suggested it is a useful biocatalyst for biodiesel preparation.

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Acknowledgements

We thank S. Zou for her technical assistance. This work was granted by the Chinese High-Tech Development Program (2006AA020203, 2007AA05Z417).

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  1. Key Laboratory of Molecular Bio-physics, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, 430074, China

    Jiangke Yang, Bo Zhang & Yunjun Yan

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  1. Jiangke Yang
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  2. Bo Zhang
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Correspondence to Yunjun Yan.

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Yang, J., Zhang, B. & Yan, Y. Cloning and Expression of Pseudomonas fluorescens 26-2 Lipase Gene in Pichia pastoris and Characterizing for Transesterification. Appl Biochem Biotechnol 159, 355–365 (2009). https://doi.org/10.1007/s12010-008-8419-5

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  • DOI: https://doi.org/10.1007/s12010-008-8419-5

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