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. 2010 Feb;76(3):971-3.
doi: 10.1128/AEM.02463-09. Epub 2009 Nov 30.

Enhanced display of lipase on the Escherichia coli cell surface, based on transcriptome analysis

Jong Hwan Baek  1 , Mee-Jung Han, Seung Hwan Lee, Sang Yup Lee
Affiliations

Enhanced display of lipase on the Escherichia coli cell surface, based on transcriptome analysis

Jong Hwan Baek et al. Appl Environ Microbiol. 2010 Feb.

Abstract

A cell surface display system was developed using Escherichia coli OmpC as an anchoring motif. The fused Pseudomonas fluorescens SIK W1 lipase was successfully displayed on the surface of E. coli cells, and the lipase activity could be enhanced by the coexpression of the gadBC genes identified by transcriptome analysis.

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Figures

FIG. 1.
FIG. 1.
Activities of lipase displayed on the surface of E. coli W3110 cells harboring pTac99A (open squares), pTacOmpC288PL (closed circles), and pTacOmpC288PL plus pHNCgadBC (open circles). Relative activity was calculated by assuming the lipase activity of the strain harboring pTacOmpC288PL at 5 h as 100%.
FIG. 2.
FIG. 2.
Outer membrane proteome profiles obtained with E. coli W3110 harboring pTac99A, pTacOmpC288PL, and pTacOmpC288PL plus pHNCgadBC. Circles indicate the position of the truncated OmpC (OmpCt)-lipase fusion protein. The middle panel shows the amino acid sequence of lipase fused to OmpCt (underlined). The signal sequence is indicated in italics. The nonredundant peptide sequences identified by nano-liquid chromatography-tandem mass spectrometry (LC/MS/MS) are indicated in boldface type. The representative peptide sequences of lipase and OmpCt are shown in the bottom panels.
See this image and copyright information in PMC

References

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