The Secretomes of Aspergillus japonicus and Aspergillus terreus Supplement the Rovabio® Enzyme Cocktail for the Degradation of Soybean Meal for Animal Feed

Autor: Delphine Grandmontagne, David Navarro, Virginie Neugnot-Roux, Simon Ladevèze, Jean-Guy Berrin

Publikováno v: Journal of Fungi, Vol 7, Iss 4, p 278 (2021)

One of the challenges of the 21st century will be to feed more than 10 billion people by 2050. In animal feed, one of the promising approaches is to use agriculture by-products such as soybean meal as it represents a rich source of proteins. However,

Externí odkaz: https://doaj.org/article/a5bf475a53f64026930eac229d7f8c22

In Vitro Synthesis and Crystallization of β-1,4-Mannan

Autor: Florent Grimaud, Simon Ladevèze, Jean-Luc Putaux, Gabrielle Potocki-Véronèse, Sandra Pizzut-Serin, Laurence Tarquis, Sandrine Morel

Publikováno v: Biomacromolecules
Biomacromolecules, 2019, 20 (2), pp.846-853. ⟨10.1021/acs.biomac.8b01457⟩
Biomacromolecules, American Chemical Society, 2019, 20 (2), pp.846-853. ⟨10.1021/acs.biomac.8b01457⟩

In vitro polymerization of β-mannans is a challenging reaction due to the steric hindrance confered by the configuration of mannosyl residues and the thermodynamic instability of the β-anomer. Whatever the approach used to date—whether chemical,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1780601f662cbdc748a787c880ea63d5
https://hal.science/hal-02177345

Lytic xylan oxidases from wood-decay fungi unlock biomass degradation

Autor: Isabelle Herpoël-Gimbert, Gerlind Sulzenbacher, Luisa Ciano, Sacha Grisel, Bernard Henrissat, Hélène Rogniaux, Bernard Cathala, Florence Chaspoul, Marie-Noëlle Rosso, Simon Ladevèze, David Ropartz, Céline Moreau, Marie Couturier, Mireille Haon, Paul H. Walton, Kristian E. H. Frandsen, Nicolas Lenfant, Jean-Guy Berrin, Mathieu Fanuel, Ana Villares, Aurore Labourel, Gideon J. Davies

Publikováno v: Nature Chemical Biology
Nature Chemical Biology, 2018, 14 (3), pp.306-310. ⟨10.1038/nchembio.2558⟩
Couturier, M, Ladevèze, S, Sulzenbacher, G, Ciano, L, Fanuel, M, Moreau, C, Villares, A, Cathala, B, Chaspoul, F, Herpoël-Gimbert, I, Grisel, S, Haon, M, Lenfant, N, Rogniaux, H, Ropartz, D, Davies, G, Rosso, M-N, Walton, P H, Henrissat, B & Berrin, J-G 2018, ' Lytic xylan oxidases from wood-decay fungi unlock biomass degradation ', Nature chemical biology, vol. 14, no. 3, pp. 306-310 . https://doi.org/10.1038/nchembio.2558
Nature Chemical Biology, Nature Publishing Group, 2018, ⟨10.1038/nchembio.2558⟩
Nature Chemical Biology, Nature Publishing Group, 2018, 14 (3), pp.306-310. ⟨10.1038/NCHEMBIO.2558⟩
Nature Chemical Biology, Nature Publishing Group, 2018, 14 (3), pp.306-310. ⟨10.1038/nchembio.2558⟩

International audience; Wood biomass is the most abundant feedstock envisioned for the development of modern biorefineries. However, the cost-effective conversion of this form of biomass into commodity products is limited by its resistance to enzymat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a0102bd5e98e22be3085552bff14c1b
https://hal.science/hal-02188478

Structural bases for N-glycan processing by mannoside phosphorylase

Autor: Gabrielle Potocki-Véronèse, Simon Ladevèze, Samuel Tranier, Pierre Roblin, Gianluca Cioci, Lionel Mourey

Publikováno v: Acta Crystallographica Section D: Biological Crystallography
'Acta Crystallographica D ', vol: 71, pages: 1335-1346 (2015)
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2015, 71 (Part 6), pp.1335-46. ⟨10.1107/S1399004715006604⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2015, 71 (Part 6), pp.1335-46. ⟨10.1107/S1399004715006604⟩
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2015, 71 (6), pp.1335-1346. ⟨10.1107/S1399004715006604⟩
Acta Crystallographica. Section D, Biological Crystallography Part 6 (71), 1335-1346. (2015)

Crystal structures of the GH130 enzyme Uhgb_MP in the apo form and in complex with mannose and N-acetylglucosamine are described and the structural determinants of the functional specificities of the enzymes involved in N-glycan breakdown by human gu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c67b32bf7575635db06e6707e655199a
https://pubmed.ncbi.nlm.nih.gov/26057673

The GH130 family of mannoside phosphorylases contains glycoside hydrolases that target beta-1,2 mannosidic linkages in Candida mannan

Autor: Simon Ladevèze, Gideon J. Davies, Elisabeth C. Lowe, Harry J. Gilbert, Alison M. Day, Gabrielle Potocki-Véronèse, Fiona Cuskin, Arnaud Baslé

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (41), ⟨10.1074/jbc.M115.681460⟩
Journal of Biological Chemistry 41 (290), 25023-25033. (2015)
The Journal of Biological Chemistry
Journal of Biological Chemistry, 2015, 290 (41), ⟨10.1074/jbc.M115.681460⟩

Background: A cohort of a family of mannose phosphorylases lack phosphate binding residues, suggesting that they display non-phosphorylase activities. Results: The non-phosphorylase enzymes were shown to be β-mannosidases. Conclusion: Replacing basi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6788326665642b1be5108a9bbbc6b65c
https://hal.archives-ouvertes.fr/hal-01184120