Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4752675 | Enzyme and Microbial Technology | 2018 | 5 Pages |
Abstract
The utility of engineering flocculation is wildly recognized in applied and environmental microbiology. We previously reported self-produced flocculation of Escherichia coli cells by overexpressing the native bcsB gene that encodes a component of the cellulose synthesis pathway. Further experiments clarified that the spontaneous E. coli flocs were proteinous, and elongation factor Ts (Tsf) was the main component. In this study, we demonstrated successful expression of a fusion protein consisting of Tsf and green fluorescence protein (GFP) on E. coli flocs. Interestingly, the percentage of Tsf-GFP in total floc protein reached approximately 15% (w/w). The proposed design of a fusion protein with Tsf enables displaying a recombinant target protein on the floc structure.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Yoshihiro Ojima, Shota Nunogami, Masayuki Azuma, Masahito Taya,