A generic system for the Escherichia coli cell-surface display of lipolytic enzymes.

@article{Becker2005AGS,
  title={A generic system for the Escherichia coli cell-surface display of lipolytic enzymes.},
  author={Stefan Becker and Sebastian Theile and Nele Heppeler and Anja Michalczyk and Alexander Wentzel and Susanne Wilhelm and K. -E. J{\"a}ger and Harald Kolmar},
  journal={FEBS letters},
  year={2005},
  volume={579 5},
  pages={1177-82}
}
EstA is an outer membrane-anchored esterase from Pseudomonas aeruginosa. An inactive EstA variant was used as an anchoring motif for the Escherichia coli cell-surface display of lipolytic enzymes. Flow cytometry analysis and measurement of lipase activity revealed that Bacillus subtilis lipase LipA, Fusarium solani pisi cutinase and one of the largest lipases presently known, namely Serratia marcescens lipase were all efficiently exported by the EstA autotransporter and also retained their… CONTINUE READING

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