Production and preliminary characterization of a fusion protein comprising streptavidin and a cellulose-binding domain
type: CreativeWork
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.
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.
author: Le, Duy Khai
language: eng
date published: 1992
date modified: 2026-07-24T05:07:26Z
provider: University of British Columbia
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of British Columbia

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2429/1584