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|Stability:||> 10 years under recommended storage conditions|
|Viscosity:||Low 0.4 cSt|
|Monosaccharides (%):||Arabinose: Xylose = 30: 70|
|Main Chain Glycosidic Linkage:||β-1,4|
|Substrate For (Enzyme):||endo-1,4-β-Xylanase|
High purity Wheat Arabinoxylan (enzyme debranched; 30% Ara) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
Prepared by controlled enzymic hydrolysis of wheat flour arabinoxylan. Essentially devoid of doubly substituted D-xylosyl residues.
Need more polysaccharides? See our carbohydrates product list.
(Trichoderma longibrachiatum) E-XYAN4 - endo-1,4-β-Xylanase M4 (Aspergillus niger) E-XYRU6 - endo-1,4-β-Xylanase (rumen microorganism) E-XYNBS - endo-1,4-β-Xylanase
(Bacillus stearothermophilus T6) E-XYNACJ - endo-1,4-β-Xylanase (Cellvibrio japonicus) E-XYLNP - endo-1,4-β-Xylanase (Neocallimastix patriciarum) E-XYLATM - endo-1,4-β-Xylanase (Thermotoga maritima) E-ABFAN - α-L-Arabinofuranosidase (Aspergillus nidulans) E-ABFBO17 - α-L-Arabinofuranosidase B17
(Bacteroides ovatus) E-ABFBO25 - α-L-Arabinofuranosidase B25
(Bacteroides ovatus) E-AFASE - α-L-Arabinofuranosidase (Aspergillus niger) E-AFAM2 - α-L-Arabinofuranosidase
(Bifidobacterium adolescentis) E-ABFUM - α-L-Arabinofuranosidase (Ustilago maydis)
Arabinoxylanase from glycoside hydrolase family 5 is a selective enzyme for production of specific arabinoxylooligosaccharides.
Falck, P., Linares-Pastén, J. A., Karlsson, E. N. & Adlercreutz, P. (2017). Food Chemistry, 242, 579-584.
An arabinose specific xylanase from glycoside hydrolase family 5 (GH5) was used to hydrolyse wheat and rye arabinoxylan, and the product profile showed that it produced arabinose substituted oligosaccharides (AXOS) having 2-10 xylose residues in the main chain but no unsubstituted xylooligosaccharides (XOS). Molecular modelling showed that the active site has an open structure and that the hydroxyl groups of all xylose residues in the active site are solvent exposed, indicating that arabinose substituents can be accommodated in the glycone as well as the aglycone subsites. The arabinoxylan hydrolysates obtained with the GH5 enzyme stimulated growth of Bifidobacterium adolescentis but not of Lactobacillus brevis. This arabinoxylanase is thus a good tool for the production of selective prebiotics.Hide Abstract