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J Chromatogr A. 2008 Jun 20;1194(2):150-4. doi: 10.1016/j.chroma.2008.04.048. Epub 2008 Apr 24.

Simple protein purification through affinity adsorption on regenerated amorphous cellulose followed by intein self-cleavage.

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Biological Systems Engineering Department, Virginia Polytechnic Institute and State University, 210-A Seitz Hall, Blacksburg, VA 24061, USA.


A simple, low-cost, and scalable protein purification method was developed by using a biodegradable regenerated amorphous cellulose (RAC) with a binding capacity of up to 365 mg protein per gram of RAC. The recombinant protein with a cellulose-binding module (CBM) tag can be specifically adsorbed by RAC. In order to avoid using costly protease and simplify purification process, a self-cleavage intein was introduced between CBM and target protein. The cleaved target protein can be liberated from the surface of RAC by intein self-cleavage occurring through a pH change from 8.0 to 6.5. Four recombinant proteins (green fluorescence protein, phosphoglucomutase, cellobiose phosphorylase, and glucan phosphorylase) have been purified successfully.

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