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

•First fungal chitin deacetylase with two chitin binding domains characterized.•Chitin binding domains shown to support enzymatic conversion of colloidal chitin.•New mode of action on chitin oligomers differing from other chitin deacetylases. Chitosan is a structurally diverse biopolymer that is com...

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Bibliographic Details
Published in:Carbohydrate polymers 2018-03, Vol.183, p.1-10
Main Authors: Hoßbach, Janina, Bußwinkel, Franziska, Kranz, Andreas, Wattjes, Jasper, Cord-Landwehr, Stefan, Moerschbacher, Bruno M.
Format: Article
Language:English
Subjects:
Chitin binding domains
Chitin deacetylase
Chitin oligomers
Chitosan
Colloidal chitin
Mode of action
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Summary:•First fungal chitin deacetylase with two chitin binding domains characterized.•Chitin binding domains shown to support enzymatic conversion of colloidal chitin.•New mode of action on chitin oligomers differing from other chitin deacetylases. 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.
ISSN:0144-8617
1879-1344
DOI:10.1016/j.carbpol.2017.11.015