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    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. © King Abdulaziz City for Science and Technology 2021.

    Citation

    Dharam Pal, Gopal Patel, Prakashkumar Dobariya, Shivraj Hariram Nile, Abhay H Pande, Uttam Chand Banerjee. Optimization of medium composition to increase the expression of recombinant human interferon-β using the Plackett-Burman and central composite design in E. coli SE1. 3 Biotech. 2021 May;11(5):226


    PMID: 33968571

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