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Arabinoxylanase from glycoside hydrolase family 5 is a selective enzyme for production of specific arabinoxylooligosaccharides

Falck, Peter, Linares-Pastén, Javier A., Karlsson, Eva Nordberg, Adlercreutz, Patrick
Food chemistry 2018 v.242 pp. 579-584
Bifidobacterium adolescentis, Lactobacillus brevis, active sites, arabinose, arabinoxylan, glycosides, hydrolysates, prebiotics, rye, solvents, wheat, xylanases, xylooligosaccharides, xylose
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.