Production of Recombinant Streptavidin and Optimization of Refolding Conditions for Recovery of Biological Activity.

ABSTRACT:

Background

Streptavidin is a protein produced by Streptomyces avidinii with strong biotin-binding ability. The non-covalent, yet strong bond between these two molecules has made it a preferable option in biological detection systems. Due to its extensive use, considerable attention is focused on streptavidin production by recombinant methods.

Methods

In this study, streptavidin was expressed in Escherichia coli (E. coli) BL21 (DE3) pLysS cells and purified by affinity chromatography. Various dialysis methods were employed to enable the protein to refold to its natural form and create a strong bond with biotin.

Results

Streptavidin was efficiently expressed in E. coli. Streptavidin attained its natural form during the dialysis phase and the

SUBMITTER: Modanloo Jouybari R 

PROVIDER: S-EPMC5940357 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature