In recombinant DNA technology, plasmid vectors carrying the insulin gene are widely used to engineer E. coli for industrial insulin production. I would like to understand the differences between this approach and using E. coli without a transformed plasmid (containing only its native genes). Specifically, how do these methods compare in terms of protein expression, efficiency of insulin yield, production cost, and scalability in industrial bioprocessing?
Transforming E. coli with the human insulin gene enables the bacteria to become a "factory" for producing human insulin, which is a crucial treatment for diabetes, so insulin are anti diabetic hormone.
The production of insulin occur by B-cells of islets of pancreas of animals, discovered by Fredrick Sanger and his coworkers and proves that insulin are smallest protein which consist of 51 amino acids and act as anti diabetic agent.
By using recombinat DNA technology, Transformed E. coli, carries a plasmid containing the human insulin gene and can synthesize human insulin (Humulin)
On the other hand Non-transformed E. coli lacks the human insulin gene and therefore cannot produce it.
Recombinant DNA technology has revolutionized biopharmaceutical production by enabling microorganisms such as Escherichia coli to produce proteins that they do not naturally synthesize. By introducing plasmid vectors carrying specific genes of interest—such as the human insulin gene—into E. coli, scientists can reprogram the bacteria to act as biological factories. These plasmids are designed with strong promoters, ribosome-binding sites, and selectable markers that enhance the transcription and translation of the inserted gene. In the context of insulin production, this technology has replaced older methods that relied on extracting and purifying insulin from animal pancreases, making the process more ethical, consistent, and scalable.
Non-transformed E. coli possess only their native genes, meaning they have no natural ability to produce insulin or any other human protein; hence, they are unsuitable for biopharmaceutical production. In contrast, transformed E. coli with plasmids carrying the insulin gene can efficiently express insulin precursors under controlled conditions, thanks to the engineered regulatory elements within the plasmid. This recombinant approach yields high levels of insulin with consistency, reducing overall production costs once the system is optimized. It also scales effectively in industrial bioreactors, as plasmid-bearing strains can be cultured to high cell densities and induced to produce large amounts of the target protein. Therefore, while native E. coli are limited to their natural metabolic functions, recombinant E. coli provide a robust, economical, and industrially scalable platform for insulin production, forming the backbone of modern insulin bioprocessing.
Why don't you read the existing literature? This honestly sounds like a homework question I'd give to my intro bio students.
Want the tl;dr answer?
Engineered E. coli can produce insulin. Non-transformed E. coli do not since the gene to make insulin is not in their genome.
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