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- Title
Expression of a lipase on the cell-surface of Escherichia coli using the OmpW anchoring motif and its application to enantioselective reactions.
- Authors
Lee, Hyuk; Park, Si; Han, Mee-Jung; Eom, Gyeong; Choi, Min-Jung; Kim, Seong; Oh, Young; Song, Bong; Lee, Seung
- 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.
- Subjects
LIPASES; ESCHERICHIA coli; ENANTIOSELECTIVE catalysis; MICROBIAL surfactants; PEPTIDES
- Publication
Biotechnology Letters, 2013, Vol 35, Issue 10, p1677
- ISSN
0141-5492
- Publication type
Article
- DOI
10.1007/s10529-013-1260-0