Volume 12, Issue 45 (11-2021)
NCMBJ 2021, 12(45): 113-127 |
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Department of Biotechnology, Golestan University, Gorgan, Iran.
Abstract: (2236 Views)
Aim and Background: Enterokinase is a gastrointestinal enzyme that acts as a protease with a specific sequence. Due to the ability of enterokinase to enzymatically digest the recombinant protein at its specific site (including the four amino acids Aspartic acid and one amino acid lysine), which is targeted at the protein, as a very useful tool for purification and separation Target protein from the non-target part is used in the pharmaceutical, food and industrial industries.
Materials and Methods: Independent variables used included OD (0.6, 1.2 and 1.8) at 600 nm, IPTG concentration (0.2, 0.5 and 0.8 mM) and The type of bacterial strain was (ShuffleT7, BL21, NICO21). The response surface methodology (RSM) in the form of a central composite scheme was used to predict independent variables on the production of enterokinase enzyme.
Results: OD equal to 1.8 at 600 nm wavelength, IPTG concentration of 0.71 mM and type of ShuffleT7 bacterial strain, LB culture medium, 2.5 mM lactose concentration and 25 ° C induction temperature, for production Recombinant enterokinase was optimized.
Discussion and Conclusion: Drug proteins play an important role in modern molecular medicine therapies. Enterokinase gene expression in the bacterial system facilitates the purification of low concentrations, so large-scale, highly purified recombinant proteins can be produced and optimized in the bacterial system.
Materials and Methods: Independent variables used included OD (0.6, 1.2 and 1.8) at 600 nm, IPTG concentration (0.2, 0.5 and 0.8 mM) and The type of bacterial strain was (ShuffleT7, BL21, NICO21). The response surface methodology (RSM) in the form of a central composite scheme was used to predict independent variables on the production of enterokinase enzyme.
Results: OD equal to 1.8 at 600 nm wavelength, IPTG concentration of 0.71 mM and type of ShuffleT7 bacterial strain, LB culture medium, 2.5 mM lactose concentration and 25 ° C induction temperature, for production Recombinant enterokinase was optimized.
Discussion and Conclusion: Drug proteins play an important role in modern molecular medicine therapies. Enterokinase gene expression in the bacterial system facilitates the purification of low concentrations, so large-scale, highly purified recombinant proteins can be produced and optimized in the bacterial system.
Type of Study: Research Article |
Subject:
Genetics
Received: 2021/08/28 | Accepted: 2021/10/28 | Published: 2021/12/22
Received: 2021/08/28 | Accepted: 2021/10/28 | Published: 2021/12/22
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