A chitin deacetylase of Podospora anserina has two functional chitin binding domains and a unique mode of action
| Autor: | Andreas Kranz, Jasper Wattjes, Stefan Cord-Landwehr, Janina Hoßbach, Franziska Bußwinkel, Bruno M. Moerschbacher |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Polymers and Plastics biology Colletotrichum lindemuthianum fungi Organic Chemistry macromolecular substances biology.organism_classification Podospora anserina Chitin deacetylase carbohydrates (lipids) Chitosan 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Chitin Biochemistry Chitin binding Acetylation Materials Chemistry Mode of action |
| Zdroj: | Europe PubMed Central |
| ISSN: | 1879-1344 |
| Popis: | Chitosan is a structurally diverse biopolymer that is commercially derived from chitin by chemical processing, but chitin deacetylases (CDAs) potentially offer a sustainable and more controllable approach allowing the production of chitosans with tailored structures and biological activities. We investigated the CDA from Podospora anserina (PaCDA) which is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. We produced recombinant PaCDA in Hansenula polymorpha for biochemical characterization and found that the catalytic domain of PaCDA is also functionally similar to C. lindemuthianum CDA, though differing in detail. When studying the enzyme's mode of action on chitin oligomers by quantitative mass-spectrometric sequencing, we found almost all possible sequences up to full deacetylation but with a clear preference for specific products. Deletion muteins lacking one or both CBDs confirmed their proposed function in supporting the enzymatic conversion of the insoluble substrate colloidal chitin. |
| Databáze: | OpenAIRE |
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