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

被引：18

作者：

Bonnin, Estelle

Daviet, Stephanie

Sorensen, Jens F.

Sibbesen, Ole

Goldson, Andrew

Juge, Nathalie

Saulnier, Luc

机构：

[1] Leurs Org & Interact, Unite Rech Polysaccharides, F-44316 Nantes 03, France

[2] Danisco AS, DK-8220 Brabrand, Denmark

[3] Danisco AS, DK-1001 Copenhagen, Denmark

[4] Inst Food Res, Norwich NR4 7UA, Norfolk, England

[5] Fac Sci & Tech St Jerome, Inst Mediterraneen Rech Nutr, UMR 1111, INRA, F-13397 Marseille 20, France

来源：

JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE | 2006年 / 86卷 / 11期

关键词：

arabinose; xylose; side chains; wheat;

D O I：

10.1002/jsfa.2501

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

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

引用

页码：1618 / 1622

页数：5

共 26 条

[1] Impact and efficiency of GH10 and GH11 thermostable endoxylanases on wheat bran and alkali-extractable arabinoxylans [J].