Sunday, May 3, 2009
3-106

Structural Studies of Enzymatic Hydrolysis of Cellulose by Neutron Scattering and Reflectivity

Michael Kent1, Jaclyn Murton2, Elizabeth Carles2, Rex Hjelm3, Bulent Akgun4, Blake A. Simmons5, James Browning6, and John Ankner6. (1) Technology Division, Joint BioEnergy Institute, 5885 Hollis Street, Fourth Floor, Emeryville, CA 94608, (2) Sandia National Laboratory, (3) Los Alamos National Laboratory, (4) NIST, (5) Energy Systems, Sandia National Laboratories, 7011 East Avenue, Livermore, CA 94551, (6) Oak Ridge National Laboratory

Improving the efficiency of enzymatic hydrolysis of cellulose is a key technological hurdle in reducing the cost of producing ethanol from lignocellulosic material. Typically, enzymatic hydrolysis proceeds to only a limited extent, high solution-to-solids ratios are required, and the rate of enzymatic hydrolysis typically decreases with time.   A range of mechanisms have been proposed to explain these phenomena including product inhibition, denaturation of enzymes, nonproductive binding, and many others.  We are studying the interaction of enzymes with cellulose to help unravel these mechanisms.  Our studies include UV absorption and circular dichroism of enzymes in solution, small angle neutron and X-ray scattering (SANS, SAXS) of cellulose during hydrolysis, and neutron reflectivity (NR) of enzymes interacting with model cellulose surfaces.  Insight from these studies should aid the development of more efficient enzyme systems and pretreatments.


Web Page: www.jbei.org