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Real-time adsorption and action of expansin on cellulose

BACKGROUND: Biological pretreatment is an environmentally safe method for disrupting recalcitrant structures of lignocellulose and thereby improving their hydrolysis efficiency. Expansin and expansin-like proteins act synergistically with cellulases during hydrolysis. A systematic analysis of the ad...

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Autores principales: Duan, Yuhao, Ma, Yuanyuan, Zhao, Xudong, Huang, Renliang, Su, Rongxin, Qi, Wei, He, Zhimin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6249958/
https://www.ncbi.nlm.nih.gov/pubmed/30479662
http://dx.doi.org/10.1186/s13068-018-1318-2
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author Duan, Yuhao
Ma, Yuanyuan
Zhao, Xudong
Huang, Renliang
Su, Rongxin
Qi, Wei
He, Zhimin
author_facet Duan, Yuhao
Ma, Yuanyuan
Zhao, Xudong
Huang, Renliang
Su, Rongxin
Qi, Wei
He, Zhimin
author_sort Duan, Yuhao
collection PubMed
description BACKGROUND: Biological pretreatment is an environmentally safe method for disrupting recalcitrant structures of lignocellulose and thereby improving their hydrolysis efficiency. Expansin and expansin-like proteins act synergistically with cellulases during hydrolysis. A systematic analysis of the adsorption behavior and mechanism of action of expansin family proteins can provide a basis for the development of highly efficient pretreatment methods for cellulosic substrates using expansins. RESULTS: Adsorption of Bacillus subtilis expansin (BsEXLX1) onto cellulose film under different conditions was monitored in real time using a quartz crystal microbalance with dissipation. A model was established to describe the adsorption of BsEXLX1 onto the film. High temperatures increased the initial adsorption rate while reducing the maximum amount of BsEXLX1 adsorbed onto the cellulose. Non-ionic surfactants (polyethylene glycol 4000 and Tween 80) at low concentrations enhanced BsEXLX1 adsorption; whereas, high concentrations had the opposite effect. However, sodium dodecyl sulfate inhibited adsorption at both low and high concentrations. We also investigated the structural changes of cellulose upon BsEXLX1 adsorption and found that BsEXLX1 adsorption decreased the crystallinity index, disrupted hydrogen bonding, and increased the surface area of cellulose, indicating greater accessibility of the substrate to the protein. CONCLUSIONS: These results increase our understanding of the interaction between expansin and cellulose, and provide evidence for expansin treatment as a promising strategy to enhance enzymatic hydrolysis of lignocellulose. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13068-018-1318-2) contains supplementary material, which is available to authorized users.
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spelling pubmed-62499582018-11-26 Real-time adsorption and action of expansin on cellulose Duan, Yuhao Ma, Yuanyuan Zhao, Xudong Huang, Renliang Su, Rongxin Qi, Wei He, Zhimin Biotechnol Biofuels Research BACKGROUND: Biological pretreatment is an environmentally safe method for disrupting recalcitrant structures of lignocellulose and thereby improving their hydrolysis efficiency. Expansin and expansin-like proteins act synergistically with cellulases during hydrolysis. A systematic analysis of the adsorption behavior and mechanism of action of expansin family proteins can provide a basis for the development of highly efficient pretreatment methods for cellulosic substrates using expansins. RESULTS: Adsorption of Bacillus subtilis expansin (BsEXLX1) onto cellulose film under different conditions was monitored in real time using a quartz crystal microbalance with dissipation. A model was established to describe the adsorption of BsEXLX1 onto the film. High temperatures increased the initial adsorption rate while reducing the maximum amount of BsEXLX1 adsorbed onto the cellulose. Non-ionic surfactants (polyethylene glycol 4000 and Tween 80) at low concentrations enhanced BsEXLX1 adsorption; whereas, high concentrations had the opposite effect. However, sodium dodecyl sulfate inhibited adsorption at both low and high concentrations. We also investigated the structural changes of cellulose upon BsEXLX1 adsorption and found that BsEXLX1 adsorption decreased the crystallinity index, disrupted hydrogen bonding, and increased the surface area of cellulose, indicating greater accessibility of the substrate to the protein. CONCLUSIONS: These results increase our understanding of the interaction between expansin and cellulose, and provide evidence for expansin treatment as a promising strategy to enhance enzymatic hydrolysis of lignocellulose. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s13068-018-1318-2) contains supplementary material, which is available to authorized users. BioMed Central 2018-11-22 /pmc/articles/PMC6249958/ /pubmed/30479662 http://dx.doi.org/10.1186/s13068-018-1318-2 Text en © The Author(s) 2018 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
Duan, Yuhao
Ma, Yuanyuan
Zhao, Xudong
Huang, Renliang
Su, Rongxin
Qi, Wei
He, Zhimin
Real-time adsorption and action of expansin on cellulose
title Real-time adsorption and action of expansin on cellulose
title_full Real-time adsorption and action of expansin on cellulose
title_fullStr Real-time adsorption and action of expansin on cellulose
title_full_unstemmed Real-time adsorption and action of expansin on cellulose
title_short Real-time adsorption and action of expansin on cellulose
title_sort real-time adsorption and action of expansin on cellulose
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6249958/
https://www.ncbi.nlm.nih.gov/pubmed/30479662
http://dx.doi.org/10.1186/s13068-018-1318-2
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