Mechanism of lignin inhibition of enzymatic biomass deconstruction [electronic resource].

Published: Washington, D.C. : United States. Dept. of Energy, 2015.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
Physical Description: 16 pages : digital, PDF file
Additional Creators: Oak Ridge National Laboratory, United States. Department of Energy, and United States. Department of Energy. Office of Scientific and Technical Information

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Summary

Here, the conversion of plant biomass to ethanol via enzymatic cellulose hydrolysis offers a potentially sustainable route to biofuel production. However, the inhibition of enzymatic activity in pretreated biomass by lignin severely limits the efficiency of this process. As a result, by performing atomic-detail molecular dynamics simulation of a biomass model containing cellulose, lignin, and cellulases (TrCel7A), we elucidate detailed lignin inhibition mechanisms. We find that lignin binds preferentially both to the elements of cellulose to which the cellulases also preferentially bind (the hydrophobic faces) and also to the specific residues on the cellulose-binding module of the cellulase that are critical for cellulose binding of TrCel7A (Y466, Y492, and Y493). In conclusion, lignin thus binds exactly where for industrial purposes it is least desired, providing a simple explanation of why hydrolysis yields increase with lignin removal.

Report Numbers

E 1.99:1327644

Subject(s)

Biomass Fuels

Other Subject(s)

Note

Published through SciTech Connect.
12/21/2015.
Biotechnology for Biofuels 8 1 ISSN 1754-6834 AM
Josh V. Vermaas; Loukas Petridis; Xianghong Qi; Roland Schulz; Benjamin Lindner; Jeremy. C. Smith.

Funding Information

AC05-00OR22725

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