The development of recombinant DNA technology in the late 20th century paved the way for the production of recombinant proteins, including growth hormones. The heterologous expression and production of recombinant growth hormones from various species, such as bovine, porcine, and ovine, have been extensively studied . The ability to produce these hormones in large quantities has significant implications for both agricultural and medical applications.
Recombinant ovine growth hormone is typically produced using Escherichia coli (E. coli) as a host organism. The process involves inserting the gene encoding the ovine growth hormone into the E. coli genome, allowing the bacteria to produce the hormone. Various factors, such as temperature, induction conditions, and media composition, are optimized to achieve high yields of biologically active roGH .
One notable study demonstrated the expression of roGH targeted to the inner membrane of E. coli using a signal sequence, DsbA. This approach resulted in a relatively high soluble protein yield of 65.3 mg/L, with the protein being easily solubilized and purified .
Ovine growth hormone consists of 190 or 191 amino acids with two disulfide bridges. It significantly enhances whole-body growth rate by stimulating protein synthesis with minimal effect on protein degradation . Additionally, it has been shown to increase milk and meat production in animals, making it a valuable tool in the agricultural industry .
The primary applications of recombinant ovine growth hormone include:
Despite the promising applications, the production and use of recombinant growth hormones face several challenges. These include regulatory hurdles, ethical concerns, and potential side effects. Future research aims to address these challenges by improving production methods, ensuring safety, and exploring new applications.