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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)1-10
Number of pages10
Early online date3 Nov 2017
Publication statusPublished - 1 Mar 2018


  • Chitin binding domains
  • Chitin deacetylase
  • Chitin oligomers
  • Chitosan
  • Colloidal chitin
  • Mode of action

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