Recombinant DNA technology coupled with overexpression is a powerful approach for
large-scale protein production in many scientific applications. In this work, E. coli cells were
transformed with the pGLO plasmid that contains genes encoding for beta-lactamase and
arabinose-induced green fluorescent protein (GFP). Following arabinose induction, GFP was
overexpressed and subsequently purified using hydrophobic interaction chromatography. The
final GFP concentration was determined to be 6.88 × 10-7 M using spectrophotometric analysis.
These results demonstrate the efficacy of DNA recombination followed by protein
overexpression and purification as an effective strategy for producing large quantities of target
proteins.
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