Expression of a lipase on the cell-surface of Escherichia coli using the OmpW anchoring motif and its application to enantioselective reactions

Hyuk Lee, Si Jae Park, Mee Jung Han, Gyeong Tae Eom, Min Jung Choi, Seong Ho Kim, Young Hoon Oh, Bong Keun Song, Seung Hwan Lee

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Microbial-surface display is the expression of proteins or peptides on the surface of cells by fusing an appropriate protein as an anchoring motif. Here, the outer membrane protein W (OmpW) was selected as a fusion partner for functional expression of Pseudomonas fluorescence SIK W1 lipase (TliA) on the cell-surface of Escherichia coli. Localization of the truncated OmpW-TliA fusion protein on the cell-surface was confirmed by immunoblotting and functional assay of lipase activity. Enantioselective hydrolysis of rac-phenylethyl butanoate by the displayed lipase resulted in optically active (R)-phenyl ethanol with 96 % enantiomeric excess and 44 % of conversion in 5 days. Thus, a small outer membrane protein OmpW, is a useful anchoring motif for displaying an active enzyme of ~50 kDa on the cell-surface and the surface-displayed lipase can be employed as an enantioselective biocatalyst in organic synthesis.

Original languageEnglish
Pages (from-to)1677-1683
Number of pages7
JournalBiotechnology Letters
Volume35
Issue number10
DOIs
StatePublished - Oct 2013

Keywords

  • Cell-surface display
  • Enantioselective biocatalyst
  • Lipase
  • Outer membrane protein

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