Structural characterization of the family GH115 α-glucuronidase from Amphibacillus xylanus yields insight into its coordinated action with α-arabinofuranosidases
| Autor: | Rosa Di Leo, Weijun Wang, Thu V. Vuong, Maija Tenkanen, Ruoyu Yan, Guillermo Toriz, Paul Gatenholm, Emma R. Master, Yang Xiu, Peter J. Stogios, Tatiana Skarina |
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| Přispěvatelé: | University of Toronto, Chalmers University of Technology, Universidad de Guadalajara, University of Helsinki, Department of Bioproducts and Biosystems, Aalto-yliopisto, Aalto University, Department of Food and Nutrition |
| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
Models Molecular Glycoside Hydrolases Stereochemistry Amphibacillus xylanus Arabinofuranosidase Bioengineering Glucuronidase Arabinoglucuronoxylan 01 natural sciences 03 medical and health sciences Hydrolysis GH115 Saccharophagus degradans 010608 biotechnology GH62 Molecular Biology Bacillaceae 030304 developmental biology chemistry.chemical_classification 11832 Microbiology and virology 0303 health sciences α biology α-Glucuronidase Aspergillus niger Active site General Medicine 414 Agricultural biotechnology α-Arabinofuranosidase biology.organism_classification Enzyme chemistry GH51 biology.protein Hemicellulases Biotechnology Streptomyces thermoviolaceus |
| Zdroj: | New Biotechnology |
| ISSN: | 1876-4347 |
| Popis: | openaire: EC/H2020/648925/EU//BHIVE The coordinated action of carbohydrate-active enzymes has mainly been evaluated for the purpose of complete saccharification of plant biomass (lignocellulose) to sugars. By contrast, the coordinated action of accessory hemicellulases on xylan debranching and recovery is less well characterized. Here, the activity of two family GH115 α-glucuronidases (SdeAgu115A from Saccharophagus degradans, and AxyAgu115A from Amphibacillus xylanus) on spruce arabinoglucuronoxylan (AGX) was evaluated in combination with an α-arabinofuranosidase from families GH51 (AniAbf51A, aka E-AFASE from Aspergillus niger) and GH62 (SthAbf62A from Streptomyces thermoviolaceus). The α-arabinofuranosidases boosted (methyl)-glucuronic acid release by SdeAgu115A by approximately 50 % and 30 %, respectively. The impact of the α-arabinofuranosidases on AxyAgu115A activity was comparatively low, motivating its structural characterization. The crystal structure of AxyAgu115A revealed increased length and flexibility of the active site loop compared to SdeAgu115A. This structural difference could explain the ability of AxyAgu115A to accommodate more highly substituted arabinoglucuronoxylan, and inform enzyme selections for improved AGX recovery and use. |
| Databáze: | OpenAIRE |
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