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Updated: Jun 24, 2026
A Comparative Analysis of Recombinant Protein Expression in Different Biofactories: Bacteria, Insect Cells and Plant Systems
Published on: March 23, 2015
Optimization of medium composition to increase the expression of recombinant human interferon-β using the
Dharam Pal1, Gopal Patel2,3, Prakashkumar Dobariya1
1Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), S.A.S. Nagar (Mohali), Sector 67, 160062 Punjab, India.
Abstract:
Recombinant human interferon-β (rhIFN-β) is therapeutically important and new commercially viable approaches are needed for its increased production. In this study, a codon-optimized gene encoding for rhIFN-β(C17S) protein was designed and expressed in E. coli SE1. As a first step of medium optimization, growth of E. coli as a function of different media components was studied. Subsequently, to optimize the media composition, a response surface methodology (RSM) was used. Our results show that optimized medium (15.0 g/L tryptone, 12.3 g/L meat extract, 1.0 g/L MgSO4 and 0.5 g/L thiamine along with minimal medium) obtained in this study provide better growth of recombinant cells and the expression level of recombinant protein was ~ 1.7-fold more than Luria-Bertani medium. The optimized medium may be utilized for the large-scale production of rhIFN-β.
