Behaviour of family 10 and 11 xylanases towards arabinoxylans with varying sturcture
Behaviour of family 10 and 11 xylanases towards arabinoxylans with varying sturcture
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DOI:
10.1002/jsfa.2501
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发表时间:
2006-08-30
影响因子:
4.1
通讯作者:
Saulnier, Luc
中科院分区:
文献类型:
--
作者:
Bonnin, Estelle;Daviet, Stephanie;Saulnier, Luc
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. (c) 2006 Society of Chemical Industry