DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, SH | ko |
dc.contributor.author | Choi, JI | ko |
dc.contributor.author | Han, MJ | ko |
dc.contributor.author | Choi, JH | ko |
dc.contributor.author | Lee, SangYup | ko |
dc.date.accessioned | 2010-11-16T07:23:18Z | - |
dc.date.available | 2010-11-16T07:23:18Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2005-04 | - |
dc.identifier.citation | BIOTECHNOLOGY AND BIOENGINEERING, v.90, pp.223 - 230 | - |
dc.identifier.issn | 0006-3592 | - |
dc.identifier.uri | http://hdl.handle.net/10203/20046 | - |
dc.description.abstract | We have developed a new cell surface display system using a major outer membrane protein of Pseudomonas aeruginosa OprF as an anchoring motif. Pseudomonas fluorescens SIK W1 lipase gene was fused to the truncated oprF gene by C-terminal deletion fusion strategy. The truncated OprF-lipase fusion protein was successfully displayed on the surface of Escherichia coli. Localization of the truncated OprF-lipase fusion protein was confirmed by western blot analysis, immunofluorescence microscopy, and whole-cell lipase activity. To examine the enzymatic characteristics of the cell surface displayed lipase, the whole-cell enzyme activity and stability were determined under various conditions. Cell surface displayed lipase showed the highest activity at 37 degrees C and pH 8.0. It retained over 80% of initial activity after incubation for a week in both aqueous solution and organic solvent. When the E. coli cells displaying lipases were used for enantio-selective resolution of racemic 1-phenylethanol in hexane, (R)-phenyl ethyl acetate was successfully obtained with the enantiomeric excess of greater than 96% in 36 h of reaction. These results suggest that E. coli cells displaying lipases using OprF as an anchoring motif can be employed for various biotechnological applications both in aqueous and nonaqueous phases. (c) 2005 Wiley Periodicals, Inc. | - |
dc.description.sponsorship | We thank Prof. J.S. Rhee and Dr. J.K. Song at KAIST for kindly providing the P. fluorescens SIK W1 strain and helpful discussions. Support by the LG Chem Chair professorship, IBM SUR program, BK21 project, and the Center for Ultramicrochemical Process Systems are appreciated. | en |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | JOHN WILEY & SONS INC | - |
dc.title | Display of lipase on the cell surface of Escherichia coli using OprF as an anchor and its application to enantioselective resolution in organic solvent | - |
dc.type | Article | - |
dc.identifier.wosid | 000227994700007 | - |
dc.identifier.scopusid | 2-s2.0-17644382948 | - |
dc.type.rims | ART | - |
dc.citation.volume | 90 | - |
dc.citation.beginningpage | 223 | - |
dc.citation.endingpage | 230 | - |
dc.citation.publicationname | BIOTECHNOLOGY AND BIOENGINEERING | - |
dc.identifier.doi | 10.1002/bit.20399 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Lee, SangYup | - |
dc.contributor.nonIdAuthor | Lee, SH | - |
dc.contributor.nonIdAuthor | Choi, JI | - |
dc.contributor.nonIdAuthor | Han, MJ | - |
dc.contributor.nonIdAuthor | Choi, JH | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | enantioselective resolution | - |
dc.subject.keywordAuthor | cell surface display | - |
dc.subject.keywordAuthor | recombinant E. coli | - |
dc.subject.keywordAuthor | OprF | - |
dc.subject.keywordAuthor | lipase | - |
dc.subject.keywordAuthor | whole-cell biocatalyst | - |
dc.subject.keywordPlus | CATALYZED KINETIC RESOLUTION | - |
dc.subject.keywordPlus | ICE-NUCLEATION PROTEIN | - |
dc.subject.keywordPlus | PSEUDOMONAS-AERUGINOSA | - |
dc.subject.keywordPlus | BIOTECHNOLOGICAL APPLICATIONS | - |
dc.subject.keywordPlus | BACTERIAL | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | BIOCATALYST | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | EPITOPE | - |
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