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Exploring why sodium lignosulfonate influenced enzymatic hydrolysis efficiency of cellulose from the perspective of substrate–enzyme adsorption
BACKGROUND: Cellulase adsorbed on cellulose is productive and helpful to produce reducing sugars in enzymatic hydrolysis of lignocellulose; however, cellulase adsorbed on lignin is non-productive. Increasing productive adsorption of cellulase on cellulose would be beneficial in improving enzymatic h...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6990501/ https://www.ncbi.nlm.nih.gov/pubmed/32015757 http://dx.doi.org/10.1186/s13068-020-1659-5 |
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author | Zheng, Wenqiu Lan, Tianqing Li, Hui Yue, Guojun Zhou, Haifeng |
author_facet | Zheng, Wenqiu Lan, Tianqing Li, Hui Yue, Guojun Zhou, Haifeng |
author_sort | Zheng, Wenqiu |
collection | PubMed |
description | BACKGROUND: Cellulase adsorbed on cellulose is productive and helpful to produce reducing sugars in enzymatic hydrolysis of lignocellulose; however, cellulase adsorbed on lignin is non-productive. Increasing productive adsorption of cellulase on cellulose would be beneficial in improving enzymatic hydrolysis. Adding lignin that was more hydrophilic in hydrolysis system could increase productive adsorption and promote hydrolysis. However, the effect mechanism is still worth exploring further. In this study, lignosulfonate (LS), a type of hydrophilic lignin, was used to study its effect on cellulosic hydrolysis. RESULTS: The effect of LS on the enzymatic hydrolysis of pure cellulose (Avicel) and lignocellulose [dilute acid (DA) treated sugarcane bagasse (SCB)] was investigated by analyzing enzymatic hydrolysis efficiency, productive and non-productive cellulase adsorptions, zeta potential and particle size distribution of substrates. The result showed that after adding LS, the productive cellulase adsorption on Avicel reduced. Adding LS to Avicel suspension could form the Avicel–LS complexes. The particles were charged more negatively and the average particle size was smaller than Avicel before adding LS. In addition, adding LS to cellulase solution formed the LS–cellulase complexes. For DA-SCB, adding LS decreased the non-productive cellulase adsorption on DA-SCB from 3.92 to 2.99 mg/g lignin and increased the productive adsorption of cellulase on DA-SCB from 2.00 to 3.44 mg/g cellulose. Besides, the addition of LS promoted the formation of LS–lignin complexes and LS–cellulase complexes, and the complexes had more negative charges and smaller average sizes than DA-SCB lignin and cellulase particles before adding LS. CONCLUSIONS: In this study, LS inhibited Avicel’s hydrolysis, but enhanced DA-SCB’s hydrolysis. This stemmed from the fact that LS could bind cellulase and Avicel, and occupied the binding sites of cellulase and Avicel. Thus, a decreased productive adsorption of cellulase on Avicel arose. Regarding DA-SCB, adding LS, which enhanced hydrolysis efficiency of DA-SCB, increased the electrostatic repulsion between DA-SCB lignin and cellulase, and therefore, decreased non-productive adsorption of cellulase on DA-SCB lignin and enhanced productive adsorption of cellulase on DA-SCB cellulose. GRAPHICAL ABSTRACT: [Image: see text] |
format | Online Article Text |
id | pubmed-6990501 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-69905012020-02-03 Exploring why sodium lignosulfonate influenced enzymatic hydrolysis efficiency of cellulose from the perspective of substrate–enzyme adsorption Zheng, Wenqiu Lan, Tianqing Li, Hui Yue, Guojun Zhou, Haifeng Biotechnol Biofuels Research BACKGROUND: Cellulase adsorbed on cellulose is productive and helpful to produce reducing sugars in enzymatic hydrolysis of lignocellulose; however, cellulase adsorbed on lignin is non-productive. Increasing productive adsorption of cellulase on cellulose would be beneficial in improving enzymatic hydrolysis. Adding lignin that was more hydrophilic in hydrolysis system could increase productive adsorption and promote hydrolysis. However, the effect mechanism is still worth exploring further. In this study, lignosulfonate (LS), a type of hydrophilic lignin, was used to study its effect on cellulosic hydrolysis. RESULTS: The effect of LS on the enzymatic hydrolysis of pure cellulose (Avicel) and lignocellulose [dilute acid (DA) treated sugarcane bagasse (SCB)] was investigated by analyzing enzymatic hydrolysis efficiency, productive and non-productive cellulase adsorptions, zeta potential and particle size distribution of substrates. The result showed that after adding LS, the productive cellulase adsorption on Avicel reduced. Adding LS to Avicel suspension could form the Avicel–LS complexes. The particles were charged more negatively and the average particle size was smaller than Avicel before adding LS. In addition, adding LS to cellulase solution formed the LS–cellulase complexes. For DA-SCB, adding LS decreased the non-productive cellulase adsorption on DA-SCB from 3.92 to 2.99 mg/g lignin and increased the productive adsorption of cellulase on DA-SCB from 2.00 to 3.44 mg/g cellulose. Besides, the addition of LS promoted the formation of LS–lignin complexes and LS–cellulase complexes, and the complexes had more negative charges and smaller average sizes than DA-SCB lignin and cellulase particles before adding LS. CONCLUSIONS: In this study, LS inhibited Avicel’s hydrolysis, but enhanced DA-SCB’s hydrolysis. This stemmed from the fact that LS could bind cellulase and Avicel, and occupied the binding sites of cellulase and Avicel. Thus, a decreased productive adsorption of cellulase on Avicel arose. Regarding DA-SCB, adding LS, which enhanced hydrolysis efficiency of DA-SCB, increased the electrostatic repulsion between DA-SCB lignin and cellulase, and therefore, decreased non-productive adsorption of cellulase on DA-SCB lignin and enhanced productive adsorption of cellulase on DA-SCB cellulose. GRAPHICAL ABSTRACT: [Image: see text] BioMed Central 2020-01-30 /pmc/articles/PMC6990501/ /pubmed/32015757 http://dx.doi.org/10.1186/s13068-020-1659-5 Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. 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 in a credit line to the data. |
spellingShingle | Research Zheng, Wenqiu Lan, Tianqing Li, Hui Yue, Guojun Zhou, Haifeng Exploring why sodium lignosulfonate influenced enzymatic hydrolysis efficiency of cellulose from the perspective of substrate–enzyme adsorption |
title | Exploring why sodium lignosulfonate influenced enzymatic hydrolysis efficiency of cellulose from the perspective of substrate–enzyme adsorption |
title_full | Exploring why sodium lignosulfonate influenced enzymatic hydrolysis efficiency of cellulose from the perspective of substrate–enzyme adsorption |
title_fullStr | Exploring why sodium lignosulfonate influenced enzymatic hydrolysis efficiency of cellulose from the perspective of substrate–enzyme adsorption |
title_full_unstemmed | Exploring why sodium lignosulfonate influenced enzymatic hydrolysis efficiency of cellulose from the perspective of substrate–enzyme adsorption |
title_short | Exploring why sodium lignosulfonate influenced enzymatic hydrolysis efficiency of cellulose from the perspective of substrate–enzyme adsorption |
title_sort | exploring why sodium lignosulfonate influenced enzymatic hydrolysis efficiency of cellulose from the perspective of substrate–enzyme adsorption |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6990501/ https://www.ncbi.nlm.nih.gov/pubmed/32015757 http://dx.doi.org/10.1186/s13068-020-1659-5 |
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