Production of Human Insulin
Since 1982, human insulin has been produced through genetic modification of bacteria, marking a significant advancement in medical technology. By inserting the human insulin gene into bacteria, scientists have enabled these modified bacteria to secrete human insulin. This method yields a purer form of insulin compared to traditional sources derived from pigs or cattle.
Insulin obtained from animal sources often contains traces of “foreign” proteins, which can potentially trigger allergic reactions in some individuals. In contrast, genetically modified insulin is devoid of such impurities, making it safer and more reliable for diabetic patients.
The process of insulin production is as follows:
The process begins with the removal of the human insulin gene using a restriction enzyme, which acts like molecular scissors to cut DNA at specific sequences.
Simultaneously, a bacterial plasmid is cut open using the same restriction enzyme, creating “sticky ends” on both the human insulin gene and the plasmid.
The insulin gene and the bacterial plasmid are joined together using another enzyme, forming a recombinant DNA molecule.
This recombinant plasmid, now containing the insulin gene, is introduced into a bacterial cell, where it replicates along with the bacterial DNA.
Inside the bacterial cell, the recombinant plasmid is replicated as the bacteria multiply, ensuring the production of insulin.
The bacterial cells containing the recombinant plasmid are transferred into a fermenter, a large vessel providing optimal conditions for microbial growth.
In the fermenter, the bacteria reproduce rapidly under controlled conditions of warmth, moisture, and oxygen, producing insulin as they multiply.
Downstream processing occurs, involving the extraction, purification, and packaging of insulin from the fermentation broth.
The pure insulin obtained from this process is suitable for medical use in treating diabetes, providing a safe and effective therapy for individuals with the condition.
