Enzymatic production of defined chitosan oligomers with a specific pattern of acetylation using a combination of chitin oligosaccharide deacetylases
| Autor: | Hamer, Stefanie Nicole, Cord-Landwehr, Stefan, Biarnés, Xevi, Planas, Antoni, Waegeman, Hendrik, Moerschbacher, Bruno Maria, Kolkenbrock, Stephan |
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| Přispěvatelé: | Universitat Ramon Llull. IQS, Universitäts- und Landesbibliothek Münster |
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Biopolímers Protein Conformation Microbiologia industrial macromolecular substances Industrial microbiology 579 - Microbiologia Article Catalysis Amidohydrolases Substrate Specificity Biopolymers Catalytic Domain ddc:570 Escherichia coli Biology Oligòmers Chitosan technology industry and agriculture Acetylation Hydrogen-Ion Concentration Recombinant Proteins carbohydrates (lipids) Chitosan oligomers Protein Binding Rhizobium |
| Zdroj: | RECERCAT (Dipòsit de la Recerca de Catalunya) Recercat: Dipósit de la Recerca de Catalunya Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) Recercat. Dipósit de la Recerca de Catalunya instname Scientific Reports |
| Popis: | Chitin and chitosan oligomers have diverse biological activities with potentially valuable applications in fields like medicine, cosmetics, or agriculture. These properties may depend not only on the degrees of polymerization and acetylation, but also on a specific pattern of acetylation (PA) that cannot be controlled when the oligomers are produced by chemical hydrolysis. To determine the influence of the PA on the biological activities, defined chitosan oligomers in sufficient amounts are needed. Chitosan oligomers with specific PA can be produced by enzymatic deacetylation of chitin oligomers, but the diversity is limited by the low number of chitin deacetylases available. We have produced specific chitosan oligomers which are deacetylated at the first two units starting from the non-reducing end by the combined use of two different chitin deacetylases, namely NodB from Rhizobium sp. GRH2 that deacetylates the first unit and COD from Vibrio cholerae that deacetylates the second unit starting from the non-reducing end. Both chitin deacetylases accept the product of each other resulting in production of chitosan oligomers with a novel and defined PA. When extended to further chitin deacetylases, this approach has the potential to yield a large range of novel chitosan oligomers with a fully defined architecture. |
| Databáze: | OpenAIRE |
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