Proteins are instrumental in all biochemical transformations that occur in any living system. Proteins perform diverse functions such as transport, transformation, stimulation, regulation, stabilization and host of other functions. To make it commercially available like the productions of insulin and industrially important enzymes, scale-up of the process is important. Traditional strategies for recombinant protein expression involve transfecting cells with a DNA vector that contains the template and then culturing the cells so that they transcribe and translate the desired protein. Typically, the cells are then lysed to extract the expressed protein for subsequent purification. Both prokaryotic and eukaryotic in vivo protein expression systems are widely used. The selection of the system depends on the type of protein.
Bacterial protein expression systems are popular because bacteria are easy to culture, grow fast and produce high yields of recombinant protein. However, multi-domain eukaryotic proteins expressed in bacteria often are non-functional because the cells are not equipped to accomplish the required post-translational modifications or molecular folding. Also, many proteins become insoluble as inclusion bodies that are very difficult to recover. Mammalian in vivo expression systems usually produce functional protein, but the yield is low, cost of production is high and mammalian cell culturing is time-consuming. In addition, in vivo systems are not conducive to either high throughput protein synthesis or expression of proteins that are toxic to host cells. Cell-free protein expression is the in vitro synthesis of protein using translation compatible extracts of whole cells. In principle, whole cell extracts contain all the macromolecular components needed for transcription, translation and even post-translational modification. These components include RNA polymerase, regulatory protein factors, transcription factors, ribosomes, and tRNA. When supplemented with cofactors, nucleotides and the specific gene template, these extracts can synthesize proteins of interest in a few hours.
The production of recombinant proteins has great potential as effective tool for research and commercial biotechnology. During the last few years, there has been an increasing interest in the field of gene regulation and protein synthesis in different systems that may be used as a novel approach for production of some important therapeutic drugs or proteins. Recent improvements/developments in this area have significantly increased its utility and enabled various groups to explore the possibilities of production of recombinant proteins, which can be directly or indirectly used for various pharmaceuticals, nutraceuticals and therapeutic purposes. Commercial production of proteins is required in the development of drugs, pharmaceuticals, nutraceuticals and industrial enzymes of commercial importance.
Serum Institute of India, Biocon, Hindustan Unilever Ltd, Kemwell Biopharma Pvt. Ltd., Thermo Scientific (Invitrogen), Sartorius AG, GE Healthcare, Bristol Myers Squibb India Ltd , Dr. Reddy’s Lab, GSK, Shantha Biotech, Novozymes, Ranbaxy, Cipla, Novortis, Pfizer, Merck, Anglo-French Drugs, Strand Life Sciences, Orchid Pharma, Jubilant Biosys, Shasun Biopharma, Quintiles, Reliance Life Sciences, United Biotech, Cadila Pharma, Advinus Therapeutics, AstraZeneca, Roche Ltd, Promega Corporation, Piramal, etc.
|Sl. No.||Name and address of the Institution||Contact Person / Details||Code|
|1||JSS College of Arts, Commerce & Science
Mysuru – 570 025.
|Dr. B. Y. Sathish Kumar