A genetically modified bacterial strain shows enhanced production of recombinant insulin but begins to accumulate misfolded protein aggregates.
What molecular mechanisms could be responsible for this, and how can biotechnology tools be used to overcome this limitation?
The accumulation of misfolded protein aggregates in a genetically modified bacterial strain producing recombinant insulin could be due to factors such as overloading the protein folding machinery, oxidative stress, or improper codon usage leading to inefficient translation.
To overcome this, biotechnology tools like chaperone co-expression, optimizing codon usage, adjusting growth conditions, or using fusion tags to enhance solubility can help improve protein folding and stability. Additionally, directing protein expression to the periplasm or using secretion pathways may reduce aggregation.