The thioredoxin system, comprising thioredoxin, thioredoxin reductase, and NADPH, is vital for maintaining a reducing environment in the cytoplasm. This system is involved in numerous cellular processes, such as DNA synthesis, repair, and defense against oxidative stress . The redox balance maintained by the thioredoxin system is crucial for cell viability and function.
E. coli is a widely used host for the production of recombinant proteins due to its well-established molecular tools, ease of cultivation, and ability to express high levels of heterologous proteins . The recombinant expression of thioredoxin reductase in E. coli allows for the production of large quantities of the enzyme, which can be purified and characterized for various applications.
Recombinant thioredoxin reductase has several applications in biotechnology and research. It can be used in studies related to redox biology, oxidative stress, and cellular metabolism. Additionally, the enzyme is valuable in the development of therapeutic agents and vaccines, as it plays a role in maintaining cellular redox homeostasis .
While the production of recombinant proteins in E. coli is generally straightforward, several challenges can arise, such as poor growth of the host, formation of inclusion bodies, and protein inactivity . Advances in molecular biology techniques have led to the development of various strategies to overcome these challenges, including the use of engineered strains, optimized expression vectors, and improved cultivation conditions .