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Mechanism of lignin inhibition of enzymatic biomass deconstruction
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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4687093/ https://www.ncbi.nlm.nih.gov/pubmed/26697106 http://dx.doi.org/10.1186/s13068-015-0379-8 |
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author | Vermaas, Josh V. Petridis, Loukas Qi, Xianghong Schulz, Roland Lindner, Benjamin Smith, Jeremy. C. |
author_facet | Vermaas, Josh V. Petridis, Loukas Qi, Xianghong Schulz, Roland Lindner, Benjamin Smith, Jeremy. C. |
author_sort | Vermaas, Josh V. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4687093 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-46870932015-12-23 Mechanism of lignin inhibition of enzymatic biomass deconstruction Vermaas, Josh V. Petridis, Loukas Qi, Xianghong Schulz, Roland Lindner, Benjamin Smith, Jeremy. C. Biotechnol Biofuels Research 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. BioMed Central 2015-12-21 /pmc/articles/PMC4687093/ /pubmed/26697106 http://dx.doi.org/10.1186/s13068-015-0379-8 Text en © Vermaas et al. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Vermaas, Josh V. Petridis, Loukas Qi, Xianghong Schulz, Roland Lindner, Benjamin Smith, Jeremy. C. Mechanism of lignin inhibition of enzymatic biomass deconstruction |
title | Mechanism of lignin inhibition of enzymatic biomass deconstruction |
title_full | Mechanism of lignin inhibition of enzymatic biomass deconstruction |
title_fullStr | Mechanism of lignin inhibition of enzymatic biomass deconstruction |
title_full_unstemmed | Mechanism of lignin inhibition of enzymatic biomass deconstruction |
title_short | Mechanism of lignin inhibition of enzymatic biomass deconstruction |
title_sort | mechanism of lignin inhibition of enzymatic biomass deconstruction |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4687093/ https://www.ncbi.nlm.nih.gov/pubmed/26697106 http://dx.doi.org/10.1186/s13068-015-0379-8 |
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