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PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses
BACKGROUND: Substrate accessibility remains a key limitation to the efficient enzymatic deconstruction of lignocellulosic biomass. Limited substrate accessibility is often addressed by increasing enzyme loading, which increases process and product costs. Alternatively, considerable efforts are under...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8928621/ https://www.ncbi.nlm.nih.gov/pubmed/35296345 http://dx.doi.org/10.1186/s13068-022-02128-8 |
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author | Monschein, Mareike Jurak, Edita Paasela, Tanja Koitto, Taru Lambauer, Vera Pavicic, Mirko Enjalbert, Thomas Dumon, Claire Master, Emma R. |
author_facet | Monschein, Mareike Jurak, Edita Paasela, Tanja Koitto, Taru Lambauer, Vera Pavicic, Mirko Enjalbert, Thomas Dumon, Claire Master, Emma R. |
author_sort | Monschein, Mareike |
collection | PubMed |
description | BACKGROUND: Substrate accessibility remains a key limitation to the efficient enzymatic deconstruction of lignocellulosic biomass. Limited substrate accessibility is often addressed by increasing enzyme loading, which increases process and product costs. Alternatively, considerable efforts are underway world-wide to identify amorphogenesis-inducing proteins and protein domains that increase the accessibility of carbohydrate-active enzymes to targeted lignocellulose components. RESULTS: We established a three-dimensional assay, PACER (plant cell wall model for the analysis of non-catalytic and enzymatic responses), that enables analysis of enzyme migration through defined lignocellulose composites. A cellulose/azo-xylan composite was made to demonstrate the PACER concept and then used to test the migration and activity of multiple xylanolytic enzymes. In addition to non-catalytic domains of xylanases, the potential of loosenin-like proteins to boost xylanase migration through cellulose/azo-xylan composites was observed. CONCLUSIONS: The PACER assay is inexpensive and parallelizable, suitable for screening proteins for ability to increase enzyme accessibility to lignocellulose substrates. Using the PACER assay, we visualized the impact of xylan-binding modules and loosenin-like proteins on xylanase mobility and access to targeted substrates. Given the flexibility to use different composite materials, the PACER assay presents a versatile platform to study impacts of lignocellulose components on enzyme access to targeted substrates. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13068-022-02128-8. |
format | Online Article Text |
id | pubmed-8928621 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-89286212022-03-23 PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses Monschein, Mareike Jurak, Edita Paasela, Tanja Koitto, Taru Lambauer, Vera Pavicic, Mirko Enjalbert, Thomas Dumon, Claire Master, Emma R. Biotechnol Biofuels Bioprod Methodology BACKGROUND: Substrate accessibility remains a key limitation to the efficient enzymatic deconstruction of lignocellulosic biomass. Limited substrate accessibility is often addressed by increasing enzyme loading, which increases process and product costs. Alternatively, considerable efforts are underway world-wide to identify amorphogenesis-inducing proteins and protein domains that increase the accessibility of carbohydrate-active enzymes to targeted lignocellulose components. RESULTS: We established a three-dimensional assay, PACER (plant cell wall model for the analysis of non-catalytic and enzymatic responses), that enables analysis of enzyme migration through defined lignocellulose composites. A cellulose/azo-xylan composite was made to demonstrate the PACER concept and then used to test the migration and activity of multiple xylanolytic enzymes. In addition to non-catalytic domains of xylanases, the potential of loosenin-like proteins to boost xylanase migration through cellulose/azo-xylan composites was observed. CONCLUSIONS: The PACER assay is inexpensive and parallelizable, suitable for screening proteins for ability to increase enzyme accessibility to lignocellulose substrates. Using the PACER assay, we visualized the impact of xylan-binding modules and loosenin-like proteins on xylanase mobility and access to targeted substrates. Given the flexibility to use different composite materials, the PACER assay presents a versatile platform to study impacts of lignocellulose components on enzyme access to targeted substrates. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13068-022-02128-8. BioMed Central 2022-03-16 /pmc/articles/PMC8928621/ /pubmed/35296345 http://dx.doi.org/10.1186/s13068-022-02128-8 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://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 | Methodology Monschein, Mareike Jurak, Edita Paasela, Tanja Koitto, Taru Lambauer, Vera Pavicic, Mirko Enjalbert, Thomas Dumon, Claire Master, Emma R. PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses |
title | PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses |
title_full | PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses |
title_fullStr | PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses |
title_full_unstemmed | PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses |
title_short | PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses |
title_sort | pacer: a novel 3d plant cell wall model for the analysis of non-catalytic and enzymatic responses |
topic | Methodology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8928621/ https://www.ncbi.nlm.nih.gov/pubmed/35296345 http://dx.doi.org/10.1186/s13068-022-02128-8 |
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