Optimization of culture conditions for the expression of three different insoluble proteins in Escherichia coli.

ABSTRACT: Recombinant protein expression for structural and therapeutic applications requires the use of systems with high expression yields. Escherichia coli is considered the workhorse for this purpose, given its fast growth rate and feasible manipulation. However, bacterial inclusion body formation remains a challenge for further protein purification. We analyzed and optimized the expression conditions for three different proteins: an anti-MICA scFv, MICA, and p19 subunit of IL-23. We used a response surface methodology based on a three-level Box-Behnken design, which included three factors: post-induction temperature, post-induction time and IPTG concentration. Comparing this information with soluble protein data in a principal component analysis revealed that insoluble and soluble proteins have

SUBMITTER: Gutierrez-Gonzalez M 

PROVIDER: S-EPMC6856375 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature