Abstract
AbstractThe 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. Copyright © 2006 Society of Chemical Industry
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