Bacterial protein expression systems are considered to be very efficient in terms of yield and cost.  However, there is no universal template in the purification of recombinant proteins from Escherichia coli.  This study evaluates purification strategies for Shiga toxin-B subunit (STxB), a pentameric-structured bacterial protein toxin produced in E. coli.  The purity obtained after each purification step was monitored using SDS-PAGE.  A previously developed purification strategy consisted of 8 purification steps, including 5 chromatography steps.  In this study, it was possible to condense the purification process into 4 steps while offering comparable purity.  This work highlights the purification capabilities of a collection of resins designed for efficient purification.

Efficient purification of a recombinant protein from Escherichia coli: A case study

247th National Meeting (2014)

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