Expression optimization, purification and in vitro characterization of human epidermal growth factor produced in Nicotiana benthamiana.

ABSTRACT: Human epidermal growth factor (hEGF) has gained clinical importance due to its ability to promote wound healing. Due to its commercial applications and high market demand, recombinant EGF has been produced in several forms. Currently, plant expression system is considered as potential alternative for low-cost recombinant protein production. Hence, this study focused on improving the production of hEGF in plants by effective gene construct design and optimizing the Agrobacterium culture conditions for high protein production. In this context, hEGF gene was cloned into plant geminiviral expression vector pBYR2e and transformed in to N. benthamiana leaves via., agroinfiltration. The recombinant hEGF was purified from the plant crude extracts by single-step affinity chroma

SUBMITTER: Hanittinan O 

PROVIDER: S-EPMC7486445 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature