Dr. Tapan K. Chaudhuri

Dr. Tapan K. Chaudhuri  |Clyto Access

Professor and Head, School of Biological Sciences, IIT New Delhi, India

Organizing Committee Member

Expertise: Chaperone assisted protein folding, Equilibrium, Kinetics and Thermodynamics of protein folding reactions, Molecular Biophysics


Dr. Tapan K. Chaudhuri received his Bachelors and Masters degree in chemistry from the University of Calcutta. He has carried out his Ph.D. degree from Bose Institute, Calcutta and post-doctoral research as JSPS fellow in the University of Tokyo, Japan, and as HHMI associate in the Yale University, USA. Later he has started his career as an Assistant Professor in the Department of Biochemical Engineering and Biotechnology, IIT Delhi and he is holding the Professor position in the newly established School of Biological Sciences, IIT Delhi. 



Title: Preparation of recombinant therapeutic protein Human Serum Albumin in Escherichia coli system for multiple applications


Human serum Albumin (HSA) is an essential protein having therapeutic applications in Trauma care and many other biotechnological applications (Kobayashi, 2006). Till now the HSA for the therapeutic usage is produced from human blood plasma. The availability of blood is limited, and also it is an unsafe source for therapeutic protein preparation because of the possibility contamination by various blood derived pathogens. Hence, there is an urgent need to explore alternative sources for the preparation of recombinant HSA. However, no alternative source has been proven to be effective so far for commercial production of rHSA because of respective limitations. So, the need for non-animal based production of rHSA is still an existing issue (Chen et al., 2013).

Escherichia coli is one of the most convenient host systems which has contributed in the production of substantial numbers of the FDA approved recombinant pharmaceuticals. Several properties of E.coli have made it a suitable expression host for recombinant protein preparation, such as the bugs grow rapidly and its culture reaches high cell density using inexpensive and simple subst¬rates (Ceccarelli et.al, Frontiers in Microbiology 2014, 5,172 1-17).The fermentation batch turnaround number for E. coli culture is far greater than any of the host systems available. Therefore, E. coli derived recombinant products have more economical potential as fermentation processes are cheaper compared to the other expression hosts available.
Despite of all the mentioned advantages, E. coli had not been successfully adopted as a host for rHSA production. The major bottleneck in exploiting E. coli as a host for rHSA production was aggregation i.e. majority of the expressed recombinant protein was forming inclusion bodies (more than 90% of the total expressed rHSA) in the E. coli cytosol studies (Lawn, 1981; Latta, 1987). Recovery of functional rHSA form inclusion body is not preferred because it is tedious, time consuming, laborious and expensive. Because of this limitation, E. coli host system was neglected for rHSA production for last few decades.
Considering the advantages of E. coli, the present work has targeted E. coli as an alternate host for rHSA production through resolving the major issue of inclusion body formation associated with it.
In this presentation we would narrate the development of a process for functional production of Human Serum Albumin in Escherichia coli system through modulation of the cellular growth, folding and environmental parameters. The significance of the newly developed process is that it has substantially improved and enhanced -expression levels as well as the functional and soluble proportion of the total expressed rHSA in the cytosolic fraction of the host (Indian Patent application No.201611045154, 2016 ").
Thus, the present work can be considered as one of the important developments in the methodology of recombinant Biopharmaceutical production for therapeutic as well as Biotechnological uses.


Related Conferences :

International Biotechnology and Pharmaceutical Industry Forum