Send to

Choose Destination
See comment in PubMed Commons below
Anal Chim Acta. 2008 Jul 28;621(2):193-9. doi: 10.1016/j.aca.2008.05.041. Epub 2008 May 27.

Bioseparation of recombinant cellulose-binding module-proteins by affinity adsorption on an ultra-high-capacity cellulosic adsorbent.

Author information

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


Low-cost protein purification methods are in high demand for mass production of low-selling price enzymes that play an important role in the upcoming bioeconomy. A simple protein purification method was developed based on affinity adsorption of a cellulose-binding module-tagged protein on regenerated amorphous cellulose (RAC) followed by modest desorption. The biodegradable cellulosic adsorbent RAC had a very high protein-binding capacity of up to 365mg of protein per gram of RAC. The specifically-bound CBM-protein on the external surface of RAC was eluted efficiently by ethyl glycol or glycerol. This protein separation method can be scaled up easily because it is based on simple solid/liquid unit operations. Five recombinant proteins (CBM-protein), regardless of intercellular or periplasmic form, were purified successfully for demonstration purpose.

[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center