完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | Chen, Y-P | en_US |
dc.contributor.author | Hwang, I-E | en_US |
dc.contributor.author | Lin, C-J | en_US |
dc.contributor.author | Wang, H-J | en_US |
dc.contributor.author | Tseng, C-P | en_US |
dc.date.accessioned | 2014-12-08T15:21:56Z | - |
dc.date.available | 2014-12-08T15:21:56Z | - |
dc.date.issued | 2012-03-01 | en_US |
dc.identifier.issn | 1364-5072 | en_US |
dc.identifier.uri | http://dx.doi.org/10.1111/j.1365-2672.2012.05232.x | en_US |
dc.identifier.uri | http://hdl.handle.net/11536/15613 | - |
dc.description.abstract | Aims: The cell-surface display of Cex, which encodes xylanase and exoglucanase from Cellulomonas fimi, was constructed on Escherichia coli using PgsA as the anchor protein. Characterization of the cell-surface display of Cex was performed. Methods and Results: PgsA was fused to the N-terminus of Cex and six histidines were utilized as spacers between the targeting and anchor proteins. Successful cell-surface display of Cex was demonstrated by Western blot and immunofluorescence analyses on E. coli C41 (DE3). According to the time-course analysis, the xylanase activity of Cex was achieved at 49 U g) 1 dry cell weight after 12 h culture at 37 degrees C. The optimal temperature and pH ranges of the cell-surface displayed protein with whole-cell were broader than the corresponding ranges of the purified form. Further determination of thermostability indicated that the half-life of cell-surface displayed Cex was 1 6 times longer than that of purified Cex at 60 degrees C. Conclusions: We have successfully developed the cell-surface display of xylanase on E. coli. The cell-surface display can enhance the stability of xylanase against changes in temperature and has the potential of becoming a whole-cell biocatalyst for industrial applications, such as biobleaching of paper and production of renewable energy. Significance and Impact of the Study: The results demonstrated that the cell-surface display of xylanase embedded in the cell membrane is more stable than that of the purified enzyme. Thus, to improve the stability of heterologous proteins production, cell-surface display using the PgsA anchor protein as a tool can be considered in E. coli. | en_US |
dc.language.iso | en_US | en_US |
dc.subject | anchor protein | en_US |
dc.subject | cell-surface display | en_US |
dc.subject | thermostability | en_US |
dc.subject | xylanase | en_US |
dc.title | Enhancing the stability of xylanase from Cellulomonas fimi by cell-surface display on Escherichia coli | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.1111/j.1365-2672.2012.05232.x | en_US |
dc.identifier.journal | JOURNAL OF APPLIED MICROBIOLOGY | en_US |
dc.citation.volume | 112 | en_US |
dc.citation.issue | 3 | en_US |
dc.citation.spage | 455 | en_US |
dc.citation.epage | 463 | en_US |
dc.contributor.department | 生物科技學系 | zh_TW |
dc.contributor.department | Department of Biological Science and Technology | en_US |
dc.identifier.wosnumber | WOS:000300044300005 | - |
dc.citation.woscount | 7 | - |
顯示於類別: | 期刊論文 |