Mechanism of lignin inhibition of enzymatic biomass deconstruction
| Autor: | Loukas Petridis, Josh V. Vermaas, Jeremy C. Smith, Roland Schulz, Benjamin Lindner, Xianghong Qi |
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| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Biomass
Cellulase macromolecular substances Management Monitoring Policy and Law Applied Microbiology and Biotechnology complex mixtures Lignin chemistry.chemical_compound Hydrolysis Biofuel Enzymatic hydrolysis Organic chemistry Cellulose Cellulose crystallinity biology Renewable Energy Sustainability and the Environment Research fungi Cel7A technology industry and agriculture food and beverages Cellulose binding General Energy chemistry Agronomy biology.protein Biotechnology |
| Zdroj: | Biotechnology for Biofuels |
| ISSN: | 1754-6834 |
| Popis: | 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. Electronic supplementary material The online version of this article (doi:10.1186/s13068-015-0379-8) contains supplementary material, which is available to authorized users. |
| Databáze: | OpenAIRE |
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