Further characterization and engineering of an 11-amino acid motif for enhancing recombinant soluble protein expression.

ABSTRACT:

Background

Escherichia coli (E. coli) is a popular system for recombinant protein production, owing to its low cost and availability of genetic tools. However, the expression of soluble recombinant proteins remains an issue. As such, various solubility-enhancing and yield-improving methods such as the addition of fusion tags have been developed. This study focuses on a small solubility tag (NT11), derived from the N-terminal domain of a duplicated carbonic anhydrase from Dunaliella species. The small size of NT11 (< 10 kDa) lowers the chance of protein folding interference and post-translation removal requirement, which ultimately minimizes cost of production.

Results

A comprehensive analysis was performed to improve the characteristics of the 11-amino acid tag. By investiga

SUBMITTER: Bi J 

PROVIDER: S-EPMC12103771 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature