Yield optimization of a heterologously expressed novel mouse macrophage protein

Parveen Pahuja, A. Srinivasan, Munish Puri

    Research output: Contribution to journalArticlepeer-review


    The large scale whole-genome sequencing projects have resulted in large numbers of un-characterized and un-annotated protein sequences. This presents an opportunity and a challenge to characterise these novel protein sequences. Structural biology has become a widely accepted methodology to help assign functions to such proteins, complementing other cellular and biochemical studies. However, most of these studies require the target protein to be produced in large quantities and in a highly pure and soluble state. The present study is an attempt to maximise production of a recombinant mouse macrophage protein (rMMP) over-expressed heterologously in Escherichia coli. Highest production of biomass and total protein (6.6 mg mL-1) was observed at 37 °C. Maximum cell disruption (89%) was observed during freeze-thawing and subsequent ultrasonication.

    Original languageEnglish
    Pages (from-to)173-181
    Number of pages9
    JournalBiosciences Biotechnology Research Asia
    Issue number1
    Publication statusPublished - Jun 2013


    • Cell disruption
    • E.coli
    • Freeze-thawing
    • Lysozyme
    • Pretreatment
    • Recombinant proteins
    • Ultra-sonication


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