Syracuse

Behaviour of family 10 and 11 xylanases towards arabinoxylans with varying structure

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Bonnin, Estelle | Daviet, Stéphanie | Sorensen, Jens | Sibbesen, Ole | Goldson, Andrew | Juge, Nathalie | Saulnier, Luc

Edité par CCSD ; Wiley -

International audience. The effect of arabinoxylan structure on xylanase activity was investigated using a range of water-soluble and water-insoluble substrates isolated from wheat flour and several xylanases from families 10 and 11 of the glycoside hydrolases. The arabinose content of the substrates affected the activity in a linear manner related to the arabinose:xylose ratio and to different extents depending on the specificity of the xylanase. The soluble/insoluble feature of the substrates had a strong impact on the enzymatic activity and different selectivities (activity on insoluble arabinoxylan vs. activity on soluble arabinoxylan) were observed. There was no relationship between specificity and selectivity of a given xylanase.

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