Production and preliminary characterization of a fusion protein comprising streptavidin and a cellulose-binding domain

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.

Name thesis:degree_name

Master of Science - MSc

Level thesis:degree_level

master's

Discipline thesis:degree_discipline

Microbiology and Immunology

Grantor dc:publisher

University of British Columbia

Year dc:date

1992

Author dc:creator

• Le, Duy Khai

Statement dc: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.

Language dc:language

eng

Handle dc:identifier

http://hdl.handle.net/2429/1584

OAI identifier oai:identifier

oai:circle.library.ubc.ca:2429/1584