Recombinant Protein Production

Proteins are fundamental biomolecules that control every biological system and play an important role in a wide range of research and industrial applications including diagnostic reagents, vaccines and therapeutic antibodies. However, isolating proteins from their natural host cells or chemical synthesis is not enough to meet the escalating demand in today’s global market. To address this challenge, recombinant protein production (RPP) is a crucial process that involves cloning and expression of gene sequences that encode specific protein molecules from an organism or strain that does not naturally produce them.

Recombinant Protein Production: Unlocking the Secrets of Biotechnology

Recombinant proteins are generated from a gene fragment that is inserted into a vector that can deliver the desired protein sequence into the host cell and trigger its transcription and translation. Recombinant proteins are then harvested from the cell cytoplasm and purified for downstream applications. To ensure that the recombinant proteins are functional and soluble, it is critical to optimize the cellular environment under which they are produced. This requires selecting the best recombinant expression system according to the protein’s characteristics and downstream requirements as well as optimizing growth conditions for the minimization of formation of insoluble inclusion bodies.

The most widely used recombinant protein expression systems are prokaryotic (Escherichia coli, Lactobacillus or Psychrophilic bacteria) and eukaryotic (mammalian cells, insect cells, yeast, filamentous fungus, and microalgae). Despite the significant progress made by these systems in recent years, they still impose severe limitations in terms of protein yield and bioactivity, primarily due to the formation of insoluble inclusion bodies. In addition, these systems require time-consuming fine-tuning of inducer concentrations in order to achieve a balance between protein yield and bioactivity.