Novel genetic control for production of recombinant protein in E. coli

Abstract

The production of functional proteins is widely used in various fields such as food, pharmaceuticals, and cosmetics industries. The production of this protein has been developed through genetic recombination technology. Escheichia coli is widely used in research and industrial environments because of its ease of use and economical [1]. However, in order to economically and efficiently mass-produce functional proteins in the field, studies such as increasing the production yield and the ratio of soluble proteins are required [2]. In this study, Xylanase was produced using E. coli.In addition, by attaching a signal peptide sequence to upstream of the xylanase sequence and linking other protein sequences to downstream of the sequence, it was attempted to confirm whether the protein production yield and the ratio of soluble protein were increased.As a result, it was confirmed that the expression and secretion level of xylanase were increased in the experimental group which the sequence was added, and soluble form was more produced.Therefore, it is shown that the level of secretion and expression level can be increased through a novel genetic control, and the ratio of soluble protein can be further increased. In addition, the transfer to the periplasm by the signal sequence can increase the protein purification process more efficiently, so it is expected that industrially and economically production will be possible.