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Mechanism of lignin inhibition of enzymatic biomass deconstruction
Authors:Josh?V?Vermaas  Loukas?Petridis  Xianghong?Qi  Roland?Schulz  Benjamin?Lindner  Email author" target="_blank">Jeremy?C?SmithEmail author
Institution:1.UT/ORNL Center for Molecular Biophysics,Oak Ridge National Laboratory,Oak Ridge,USA;2.Center for Biophysics and Quantitative Biology,University of Illinois at Urbana-Champaign,Urbana,USA;3.Department of Biochemistry and Cellular and Molecular Biology,University of Tennessee,Knoxville,USA;4.University of Tennessee/Oak Ridge National Laboratory Center for Molecular Biophysics,Oak Ridge,USA
Abstract:

Background

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.

Results

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).

Conclusions

Lignin thus binds exactly where for industrial purposes it is least desired, providing a simple explanation of why hydrolysis yields increase with lignin removal.
Keywords:
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