- Library Home /
- Search Collections /
- Open Collections /
- Browse Collections /
- UBC Theses and Dissertations /
- Production and preliminary characterization of a fusion...
Open Collections
UBC Theses and Dissertations
UBC Theses and Dissertations
Production and preliminary characterization of a fusion protein comprising streptavidin and a cellulose-binding domain Le, Duy Khai
Abstract
The cellulose-binding domain of exoglucanase Cex (CBDCex) from Cellulomonas fimi can be fused to heterologous proteins. The fusion proteins can be purified by affinity chromatography on cellulose or immobilized on cellulose (Ong et al., 1989b). Streptavidin, a protein produced by Streptomyces avidinii, binds to the water-soluble vitamin, D-biotin, with remarkably high affinity. The strong and specific biotin-binding affinity of streptavidin offers a variety of applications in biotechnology (Wilchek and Bayer, 1990). The streptavidin gene was fused in frame to the CBDcex coding sequence and the gene fusion expressed to give a chimeric protein comprising streptavidin and the cellulose-binding domain. The fusion protein was overexpresed in E. coli and formed inclusion bodies. The soluble renatured protein recovered from the inclusion bodies bound both biotin and cellulose. It could be used to bind biotinylated proteins to cellulose.
Item Metadata
Title |
Production and preliminary characterization of a fusion protein comprising streptavidin and a cellulose-binding domain
|
Creator | |
Publisher |
University of British Columbia
|
Date Issued |
1992
|
Description |
The cellulose-binding domain of exoglucanase Cex (CBDCex) from Cellulomonas fimi can be fused to heterologous proteins. The fusion proteins can be purified by affinity chromatography on cellulose or immobilized on cellulose (Ong et al., 1989b). Streptavidin, a protein produced by Streptomyces avidinii, binds to the water-soluble vitamin, D-biotin, with remarkably high affinity. The strong and specific biotin-binding affinity of streptavidin offers a variety of applications in biotechnology (Wilchek and Bayer, 1990). The streptavidin gene was fused in frame to the CBDcex coding sequence and the gene fusion expressed to give a chimeric protein comprising streptavidin and the cellulose-binding domain. The fusion protein was overexpresed in E. coli and formed inclusion bodies. The soluble renatured protein recovered from the inclusion bodies bound both biotin and cellulose. It could be used to bind biotinylated proteins to cellulose.
|
Extent |
6425753 bytes
|
Genre | |
Type | |
File Format |
application/pdf
|
Language |
eng
|
Date Available |
2008-08-29
|
Provider |
Vancouver : University of British Columbia Library
|
Rights |
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
|
DOI |
10.14288/1.0086335
|
URI | |
Degree | |
Program | |
Affiliation | |
Degree Grantor |
University of British Columbia
|
Graduation Date |
1993-05
|
Campus | |
Scholarly Level |
Graduate
|
Aggregated Source Repository |
DSpace
|
Item Media
Item Citations and Data
Rights
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.