Materials Map

Discover the materials research landscape. Find experts, partners, networks.

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The Materials Map is an open tool for improving networking and interdisciplinary exchange within materials research. It enables cross-database search for cooperation and network partners and discovering of the research landscape.

The dashboard provides detailed information about the selected scientist, e.g. publications. The dashboard can be filtered and shows the relationship to co-authors in different diagrams. In addition, a link is provided to find contact information.

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The Materials Map is still under development. In its current state, it is only based on one single data source and, thus, incomplete and contains duplicates. We are working on incorporating new open data sources like ORCID to improve the quality and the timeliness of our data. We will update Materials Map as soon as possible and kindly ask for your patience.

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in Cooperation with on an Cooperation-Score of 37%

Topics

Publications (1/1 displayed)

  • 2009In vitro model assemblies to study the impact of lignin-carbohydrate interactions on the enzymatic conversion of Xylan40citations

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Chart of shared publication
Barakat, Abdellatif
1 / 15 shared
Puteaux, Jean-Luc
1 / 2 shared
Chabbert, Brigitte
1 / 22 shared
Donohue, Michael O.
1 / 1 shared
Cathala, Bernard
1 / 15 shared
Boukari, Imen
1 / 3 shared
Saake, Bodo
1 / 5 shared
Chart of publication period
2009

Co-Authors (by relevance)

  • Barakat, Abdellatif
  • Puteaux, Jean-Luc
  • Chabbert, Brigitte
  • Donohue, Michael O.
  • Cathala, Bernard
  • Boukari, Imen
  • Saake, Bodo
OrganizationsLocationPeople

article

In vitro model assemblies to study the impact of lignin-carbohydrate interactions on the enzymatic conversion of Xylan

  • Barakat, Abdellatif
  • Puteaux, Jean-Luc
  • Chabbert, Brigitte
  • Remond, Caroline
  • Donohue, Michael O.
  • Cathala, Bernard
  • Boukari, Imen
  • Saake, Bodo
Abstract

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.

Topics
  • nanocomposite
  • impedance spectroscopy
  • compound
  • polymer
  • lignin
  • molecular weight
  • alcohol