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Interplays of enzyme, substrate, and surfactant on hydrolysis of native lignocellulosic biomass
Tracking enzyme, substrate, and surfactant interactions to reach maximum reducing sugar production during enzymatic hydrolysis of plant biomass may provide a better understanding of factors that limit the lignocellulosic material degradation in native rice straw. In this study, enzymes (Cellic Ctec2...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8806531/ https://www.ncbi.nlm.nih.gov/pubmed/34369275 http://dx.doi.org/10.1080/21655979.2021.1961662 |
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author | Lee, Sengthong Akeprathumchai, Saengchai Bundidamorn, Damkerng Salaipeth, Lakha Poomputsa, Kanokwan Ratanakhanokchai, Khanok Chang, Ken-Lin Phitsuwan, Paripok |
author_facet | Lee, Sengthong Akeprathumchai, Saengchai Bundidamorn, Damkerng Salaipeth, Lakha Poomputsa, Kanokwan Ratanakhanokchai, Khanok Chang, Ken-Lin Phitsuwan, Paripok |
author_sort | Lee, Sengthong |
collection | PubMed |
description | Tracking enzyme, substrate, and surfactant interactions to reach maximum reducing sugar production during enzymatic hydrolysis of plant biomass may provide a better understanding of factors that limit the lignocellulosic material degradation in native rice straw. In this study, enzymes (Cellic Ctec2 cellulase and Cellic Htec2 xylanase) and Triton X-100 (surfactant) were used as biocatalysts for cellulose and xylan degradation and as a lignin blocking agent, respectively. The response surface model (R(2) = 0.99 and R(2)-adj = 0.97) indicated that Cellic Ctec2 cellulase (p < 0.0001) had significant impacts on reducing sugar production, whereas Cellic Htec2 xylanase and Triton X-100 had insignificant impacts on sugar yield. Although FTIR analysis suggested binding of Triton X-100 to lignin surfaces, the morphological observation by SEM revealed similar surface features (i.e., smooth surfaces with some pores) of rice straw irrespective of Triton X-100. The reducing sugar yields from substrate hydrolysis with or without the surfactant were comparable, suggesting similar exposure of polysaccharides accessible to the enzymes. The model analysis and chemical and structural evidence suggest that there would be no positive effects on enzymatic hydrolysis by blocking lignins with Triton X-100 if high lignin coverage exists in the substrate due to the limited availability of hydrolyzable polysaccharides. |
format | Online Article Text |
id | pubmed-8806531 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-88065312022-02-02 Interplays of enzyme, substrate, and surfactant on hydrolysis of native lignocellulosic biomass Lee, Sengthong Akeprathumchai, Saengchai Bundidamorn, Damkerng Salaipeth, Lakha Poomputsa, Kanokwan Ratanakhanokchai, Khanok Chang, Ken-Lin Phitsuwan, Paripok Bioengineered Research Paper Tracking enzyme, substrate, and surfactant interactions to reach maximum reducing sugar production during enzymatic hydrolysis of plant biomass may provide a better understanding of factors that limit the lignocellulosic material degradation in native rice straw. In this study, enzymes (Cellic Ctec2 cellulase and Cellic Htec2 xylanase) and Triton X-100 (surfactant) were used as biocatalysts for cellulose and xylan degradation and as a lignin blocking agent, respectively. The response surface model (R(2) = 0.99 and R(2)-adj = 0.97) indicated that Cellic Ctec2 cellulase (p < 0.0001) had significant impacts on reducing sugar production, whereas Cellic Htec2 xylanase and Triton X-100 had insignificant impacts on sugar yield. Although FTIR analysis suggested binding of Triton X-100 to lignin surfaces, the morphological observation by SEM revealed similar surface features (i.e., smooth surfaces with some pores) of rice straw irrespective of Triton X-100. The reducing sugar yields from substrate hydrolysis with or without the surfactant were comparable, suggesting similar exposure of polysaccharides accessible to the enzymes. The model analysis and chemical and structural evidence suggest that there would be no positive effects on enzymatic hydrolysis by blocking lignins with Triton X-100 if high lignin coverage exists in the substrate due to the limited availability of hydrolyzable polysaccharides. Taylor & Francis 2021-08-08 /pmc/articles/PMC8806531/ /pubmed/34369275 http://dx.doi.org/10.1080/21655979.2021.1961662 Text en © 2021 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) ), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Lee, Sengthong Akeprathumchai, Saengchai Bundidamorn, Damkerng Salaipeth, Lakha Poomputsa, Kanokwan Ratanakhanokchai, Khanok Chang, Ken-Lin Phitsuwan, Paripok Interplays of enzyme, substrate, and surfactant on hydrolysis of native lignocellulosic biomass |
title | Interplays of enzyme, substrate, and surfactant on hydrolysis of native lignocellulosic biomass |
title_full | Interplays of enzyme, substrate, and surfactant on hydrolysis of native lignocellulosic biomass |
title_fullStr | Interplays of enzyme, substrate, and surfactant on hydrolysis of native lignocellulosic biomass |
title_full_unstemmed | Interplays of enzyme, substrate, and surfactant on hydrolysis of native lignocellulosic biomass |
title_short | Interplays of enzyme, substrate, and surfactant on hydrolysis of native lignocellulosic biomass |
title_sort | interplays of enzyme, substrate, and surfactant on hydrolysis of native lignocellulosic biomass |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8806531/ https://www.ncbi.nlm.nih.gov/pubmed/34369275 http://dx.doi.org/10.1080/21655979.2021.1961662 |
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