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Hoßbach J, Bußwinkel F, Kranz A, et al. A chitin deacetylase of Podospora anserina has two functional chitin binding domains and a unique mode of action. Carbohydr Polym. 2017;183:1-10doi: 10.1016/j.carbpol.2017.11.015.
Hoßbach, J., Bußwinkel, F., Kranz, A., Wattjes, J., Cord-Landwehr, S., & Moerschbacher, B. M. (2018). A chitin deacetylase of Podospora anserina has two functional chitin binding domains and a unique mode of action. Carbohydrate polymers, 1831-10. https://doi.org/10.1016/j.carbpol.2017.11.015
Hoßbach, Janina, et al. "A chitin deacetylase of Podospora anserina has two functional chitin binding domains and a unique mode of action." Carbohydrate polymers vol. 183 (2018): 1-10. doi: https://doi.org/10.1016/j.carbpol.2017.11.015
Hoßbach J, Bußwinkel F, Kranz A, Wattjes J, Cord-Landwehr S, Moerschbacher BM. A chitin deacetylase of Podospora anserina has two functional chitin binding domains and a unique mode of action. Carbohydr Polym. 2018 Mar 01;183:1-10. doi: 10.1016/j.carbpol.2017.11.015. Epub 2017 Nov 03. PMID: 29352863.
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Carbohydr Polym. 2018 Mar 01;183:1-10. doi: 10.1016/j.carbpol.2017.11.015. Epub 2017 Nov 03.

A chitin deacetylase of Podospora anserina has two functional chitin binding domains and a unique mode of action.

Carbohydrate polymers

Janina Hoßbach, Franziska Bußwinkel, Andreas Kranz, Jasper Wattjes, Stefan Cord-Landwehr, Bruno M Moerschbacher

Affiliations

  1. Institute for Biology and Biotechnology of Plants, University of Münster, Schlossplatz 8, 48143 Münster, Germany. Electronic address: [email protected].
  2. Institute for Biology and Biotechnology of Plants, University of Münster, Schlossplatz 8, 48143 Münster, Germany. Electronic address: [email protected].
  3. ARTES Biotechnology GmbH, Elisabeth-Selbert-Str. 9, 40764 Langenfeld, Germany. Electronic address: [email protected].
  4. Institute for Biology and Biotechnology of Plants, University of Münster, Schlossplatz 8, 48143 Münster, Germany. Electronic address: [email protected].
  5. Institute for Biology and Biotechnology of Plants, University of Münster, Schlossplatz 8, 48143 Münster, Germany. Electronic address: [email protected].
  6. Institute for Biology and Biotechnology of Plants, University of Münster, Schlossplatz 8, 48143 Münster, Germany. Electronic address: [email protected].

PMID: 29352863 DOI: 10.1016/j.carbpol.2017.11.015

Abstract

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.

Copyright © 2017. Published by Elsevier Ltd.

Keywords: Chitin binding domains; Chitin deacetylase; Chitin oligomers; Chitosan; Colloidal chitin; Mode of action

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