The Effect of DMSO, IPTG and Incubation Temperature on Growth Hormone Protein Expression in E.coli

Document Type : Article

Authors

1 Ph.D. Candidate, Biotechnology Research Center, Malek-Ashtar University of Technology, Tehran, Iran

2 Associate Professor of Biophysics, Biotechnology Research Center, Malek-Ashtar University of Technology, Tehran, Iran

3 Assistant Professor of Biophysics, Biotechnology Research Center, Malek-Ashtar University of Technology, Tehran, Iran

Abstract

hormone as a drug product is not limited to its application to the topic of short-term treatment of pediatric patients is made recombinant. Since the low expression of this heavy protein in the recombinant state influences its effective extraction, various changes have been made on this protein in the culture and expression stage. In this study, optimization based on the concentration of DMSO additive in a culture medium, incubation temperature, and induction concentration have been investigated. The results of PAGE-SDS showed a good percentage for 1% dimethyl sulfoxide and suitable temperature for incubation of 16 ° C and an appropriate concentration for Isopropylthiogalactoside inducer 0.1 mM. In the next step, the culture specimen was optimized with 10 recombinant proteins. To ensure the correct cultivation and optimization of recombinant growth hormone, the secondary protein structure of the protein has been verified and verified using Circular Dichroism Spectroscopy (CD) and subsequently verified using the intrinsic fluorescence technique of the third protein structure.

Keywords

Biomacromolecular Journal
Volume 7, Issue 3
December 2021
Pages 86-92

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