Academic Journal
In vitro model assemblies to study the impact of lignin-carbohydrate interactions on the enzymatic conversion of Xylan
| العنوان: | In vitro model assemblies to study the impact of lignin-carbohydrate interactions on the enzymatic conversion of Xylan |
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| المؤلفون: | Boukari, Imen, Putaux, Jean-Luc, Cathala, Bernard, Barakat, Abdellatif, Saake, Bodo, Rémond, Caroline, O Donohue, Michael, Chabbert, Brigitte |
| المساهمون: | Fractionnement des AgroRessources et Environnement (FARE), Université de Reims Champagne-Ardenne (URCA)-Institut National de la Recherche Agronomique (INRA), Centre de Recherches sur les Macromolécules Végétales (CERMAV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS), Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Johann Heinrich von Thünen Institut, Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | ISSN: 1525-7797. |
| بيانات النشر: | HAL CCSD American Chemical Society |
| سنة النشر: | 2009 |
| المجموعة: | Université de Reims Champagne-Ardenne: Archives Ouvertes (HAL) |
| مصطلحات موضوعية: | endoxylanase, [SDV.IDA]Life Sciences [q-bio]/Food engineering, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, [SDV]Life Sciences [q-bio], [SDE]Environmental Sciences |
| الوصف: | International audience ; Endo-beta-1,4-xylanases (EC 3.2.1.8) are the main enzymes involved in the hydrolysis of xylans, the most abundant hemicelluloses in plant. biomass. However, the development of efficient endoxylanases for use in biorefinery processes is currently hampered by insufficient knowledge regarding the impact of the cell wall network organization on the action of the enzyme at the supramolecular level. The action pattern of a GH11 endoxylanase from Thermobacillus xylanilyticus (Tx-xyl) was investigated by means of in vitro reconstituted model systems which can mimic certain cell wall structures. The action of Tx-xyl was evaluated on polymer assemblies displaying increasing complexity using delignified glucuronoarabinoxylan (GAX), then GAX-DHP model complexes obtained by oxidative polymerization of coniferyl alcohol into dehydrogenation polymers (DHP: lignin model compounds) in the presence of GAX At a high concentration of GAX, interchain associations are formed leading to high molecular weight aggregates. These structures did not appear to affect the action of endoxylanase, which induces disaggregation of the self-aggregates along with polymer depolymerization. To mimic lignin-carbohydrate interactions, two different GAX-DHP nanocomposites were prepared and incubated with endoxylanase. In both cases, free GAX was hydrolyzed, while the GAX-DHP complexes appeared to be resistant. In the case of the noncovalently linked GAX-DHP(ZL) complexes, enzyme action favored a decrease in particle size, owing to the removal of their relatively exposed carbohydrate chains, whereas the complex supramolecular organization of the covalently linked GAX-DHP(ZT) complexes severely hampers the enzyme's access to carbohydrate. Overall, these results establish the negative impact of DHP on the endoxylanase action and provide new knowledge regarding the limitations of the enzyme action in the lignocellulose bioconversion processes. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | hal-02666812; https://hal.inrae.fr/hal-02666812; PRODINRA: 50512; WOS: 000269671200014 |
| DOI: | 10.1021/bm9004518 |
| الاتاحة: | https://hal.inrae.fr/hal-02666812 https://doi.org/10.1021/bm9004518 |
| رقم الانضمام: | edsbas.BE39B7C9 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1021/bm9004518 |
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