Cloning and expression of Pseudomonas fluorescens 26-2 lipase gene in Pichia pastoris and characterizing for transesterification.
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 Mut(S) and Mut(+) phenotypes were acquired. The characteristics and the transesterification capacity shown by this enzyme suggested it is a useful biocatalyst for biodiesel preparation.
Yang
Jiangke
J
Key Laboratory of Molecular Bio-physics, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China.
Zhang
Bo
B
Yan
Yunjun
Y
D003001:Cloning, Molecular / Q000379:methods*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004951:Esterification; D004952:Esters / Q000737:chemistry; D015870:Gene Expression / Q000502:physiology; D008049:Lipase / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism; D010843:Pichia / Q000201:enzymology* / Q000235:genetics*; D011551:Pseudomonas fluorescens / Q000201:enzymology* / Q000235:genetics*; D011994:Recombinant Proteins / Q000737:chemistry* / Q000378:metabolism
D004952:Esters; D011994:Recombinant Proteins; D008049:Lipase